Merck
CN
All Photos(2)

Documents

Safety Information

P1867

Sigma-Aldrich

Plasmin from human plasma

lyophilized powder, ≥2.0 units/mg protein

Sign Into View Organizational & Contract Pricing

Synonym(s):
Fibrinolysin
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42030239
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥2.0 units/mg protein

impurities

HIV, Hepatitis B and Hepatitis C, tested negative

UniProt accession no.

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

human ... PLG(5340)

Looking for similar products? Visit Product Comparison Guide

General description

Plasmin functions as a key enzyme of the fibrinolytic cascade, and is also important in inflammation processes.

Application

A complex between plasmin and an inhibitor has been isolated in a study via affinity chromatography from urokinase-activated human plasma. It has also been used in a study to investigate activation of human epithelial sodium channel (ENaC) by plasmin and chymotrypsin.

Biochem/physiol Actions

It is inhibited by α 2-antiplasmin and its interaction with fibrin is blocked. It digests the N-terminal region of the cytoplasmic protein αsynuclein preventing its uptake by surrounding cells.
Plasmin exhibits preferential cleavage at the carboxyl side of lysine and arginine residues with higher selectivity than trypsin. Converts polymerized fibrin into soluble products.
pH Optimum: 8.5
pH 7.5: ~40% of maximal activity, pH 9.5: ~50% of maximal activity
Temperature Optimum: 37 °C with rapid inactivation at 56 °C

Packaging

Package size based on protein content

Unit Definition

One unit will produce one μmole of p-Nitroanilide from D-Val-Leu-Lys-p-Nitroanilide per minute at pH 7.5 at 37 °C.

Physical form

Lyophilized powder containing sodium phosphate, mannitol, and NaCl.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Documents related to the products that you have purchased in the past have been gathered in the Document Library for your convenience.

Visit the Document Library

Difficulty Finding Your Product Or Lot/Batch Number?

Product numbers are combined with Pack Sizes/Quantity when displayed on the website (example: T1503-25G). Please make sure you enter ONLY the product number in the Product Number field (example: T1503).

Example:

T1503
Product Number
-
25G
Pack Size/Quantity

Additional examples:

705578-5MG-PW

PL860-CGA/SHF-1EA

MMYOMAG-74K-13

1000309185

enter as 1.000309185)

Having trouble? Feel free to contact Technical Service for assistance.

Lot and Batch Numbers can be found on a product's label following the words 'Lot' or 'Batch'.

Aldrich Products

  • For a lot number such as TO09019TO, enter it as 09019TO (without the first two letters 'TO').

  • For a lot number with a filling-code such as 05427ES-021, enter it as 05427ES (without the filling-code '-021').

  • For a lot number with a filling-code such as STBB0728K9, enter it as STBB0728 without the filling-code 'K9'.

Not Finding What You Are Looking For?

In some cases, a COA may not be available online. If your search was unable to find the COA you can request one.

Request COA

  1. Which document(s) contains shelf-life or expiration date information for a given product?

    If available for a given product, the recommended re-test date or the expiration date can be found on the Certificate of Analysis.

  2. How do I get lot-specific information or a Certificate of Analysis?

    The lot specific COA document can be found by entering the lot number above under the "Documents" section.

  3. How do I find price and availability?

    There are several ways to find pricing and availability for our products. Once you log onto our website, you will find the price and availability displayed on the product detail page. You can contact any of our Customer Sales and Service offices to receive a quote.  USA customers:  1-800-325-3010 or view local office numbers.

  4. What is the Department of Transportation shipping information for this product?

    Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product. 

  5. Can Product P1867, Plasmin from human plasma, be stored?

    Sigma has not evaluated the solution stability of plasmin solutions.It is best to prepare solutions fresh.

  6. Does Product P1867, Plasmin from human plasma, have a recommended retest date?

    If a product has a recommended retest date this would be on the Certificate of Analysis found at our website.  If no recommended retest date is found on the Certificate of Analysis, then the guarantee of quality is one year from the time of delivery for unopened bottles stored at the recommended temperature.

  7. Is there a conversion to International Units (I.U.) for Product P1867, Plasmin from human plasma?

    Sigma has not evaluated the activity of this enzyme in I.U., nor do we have a conversion factor.

  8. What is the molecular weight of Product P1867, Plasmin from human plasma?

    The molecular weight of this dimeric protein was reported to be 75,400 Daltons. Reference is: The Plasma Proteins, Volume 1, 2nd ed., Putnam, F.W., ed., p. 66 (1975).

  9. What is Product P1867, Plasmin from human plasma, soluble in?

    It is soluble in water.

  10. Can you provide a method of production for Product P1867 - Plasmin?

    Product P1867 - Plasmin from human plasma is from an outside supplier and the manufacturing process is considered proprietary.  The product is activated with Streptokinase and this enzyme is removed in the final steps of the purification.  The product is >95% by SDS PAGE. The product is >3% protein (the exact value will be on the lot specific Certificate of Analysis).  This material is lyophilized from 20 mM sodium phosphate (pH 7.4), containing 10 mg/ml D-mannitol and 10 mg/ml NaCl.  The lyophyllization buffer will contribute a significant amount of solids to the product.  The product package size is based on protein content.

  11. My question is not addressed here, how can I contact Technical Service for assistance?

    Ask a Scientist here.

S Müllertz et al.
The Biochemical journal, 159(3), 545-553 (1976-12-01)
A complex between plasmin and an inhibitor was isolated by affinity chromatography from urokinase-activated human plasma. The complex did not react with antibodies against any of the known proteinase inhibitors in plasma. A rabbit antiserum against the complex was produced.
Efrat Shavit-Stein et al.
PloS one, 16(3), e0248431-e0248431 (2021-03-16)
Ischemic stroke is a common and debilitating disease with limited treatment options. Protease activated receptor 1 (PAR1) is a fundamental cell signaling mediator in the central nervous system (CNS). It can be activated by many proteases including thrombin and plasmin
Tatiana Syrovets et al.
Journal of leukocyte biology, 92(3), 509-519 (2012-05-09)
The serine protease plasmin generated from its zymogen plasminogen is best known for its function as a key enzyme of the fibrinolytic cascade. However, beyond fibrinolysis, plasmin has a number of crucial functions in a variety of processes, including inflammation.
Sara Raimondi et al.
The Journal of biological chemistry, 295(33), 11379-11387 (2020-06-24)
Systemic amyloidosis caused by extracellular deposition of insoluble fibrils derived from the pathological aggregation of circulating proteins, such as transthyretin, is a severe and usually fatal condition. Elucidation of the molecular pathogenic mechanism of the disease and discovery of effective
Silke Haerteis et al.
The Journal of general physiology, 140(4), 375-389 (2012-09-12)
Proteolytic activation of the epithelial sodium channel (ENaC) involves cleavage of its γ subunit in a critical region targeted by several proteases. Our aim was to identify cleavage sites in this region that are functionally important for activation of human

Protocols

Enzymatic Assay of Plasmin with D-Val-Leu-Lys-p-Nitroanilide Dihydrochloride

Enzymatic Assay of Plasmin with D-Val-Leu-Lys-p-Nitroanilide Dihydrochloride

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service