WH0005223M1
Monoclonal Anti-PGAM1 antibody produced in mouse
clone 2G1-A6, purified immunoglobulin, buffered aqueous solution
别名:
Anti-PGAMA, Anti-phosphoglycerate mutase 1 (brain)
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NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
2G1-A6, monoclonal
Application:
ELISA (i), WB
Citations:
5
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2G1-A6, monoclonal
form
buffered aqueous solution
species reactivity
human
technique(s)
indirect ELISA: suitable, western blot: 1-5 μg/mL
isotype
IgG1κ
GenBank accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... PGAM1(5223)
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General description
Phosphoglycerate mutase 1 (PGAM1) is an important glycolytic enzyme. This gene is located on human chromosome 10q24.
Immunogen
PGAM1 (AAH11678.1, 1 a.a. ~ 254 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Sequence
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKAKK
Sequence
MAAYKLVLIRHGESAWNLENRFSGWYDADLSPAGHEEAKRGGQALRDAGYEFDICFTSVQKRAIRTLWTVLDAIDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEAQVKIWRRSYDVPPPPMEPDHPFYSNISKDRRYADLTEDQLPSCESLKDTIARALPFWNEEIVPQIKEGKRVLIAAHGNSLRGIVKHLEGLSEEAIMELNLPTGIPIVYELDKNLKPIKPMQFLGDEETVRKAMEAVAAQGKAKK
Application
Monoclonal Anti-PGAM1 antibody has been used in western blotting.
Biochem/physiol Actions
Phosphoglycerate mutase 1 (PGAM1) participates in glycolysis, pentose phosphate pathway and serine biosynthesis in cancer cells. It helps to convert 3-phosphoglycerate (3-PG) into 2-PG in glycolysis. PGAM1 is essential to support glycolysis for normal cell activities.
Physical form
Solution in phosphate buffered saline, pH 7.4
Legal Information
GenBank is a registered trademark of United States Department of Health and Human Services
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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存储类别
12 - Non Combustible Liquids
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
新产品
此项目有
Identification of proteins with different abundance associated with cell migration and proliferation in leiomyoma interstitial fluid by proteomics
Ura B, et al.
Oncology Letters, 13(5), 3912-3920 (2017)
Bisphosphoglycerate mutase controls serine pathway flux via 3-phosphoglycerate
Oslund RC, et al.
Nature Chemical Biology, 13(10), 1081-1087 (2017)
Phosphoglycerate mutase 1 regulates dNTP pool and promotes homologous recombination repair in cancer cells
Qu J, et al.
The Journal of Cell Biology, 216(2), 409-424 (2017)
CHUK, a conserved helix-loop-helix ubiquitous kinase, maps to human chromosome 10 and mouse chromosome 19
Mock BA, et al.
Genomics, 27(2), 348-351 (1995)
Blendi Ura et al.
Oncology letters, 13(5), 3912-3920 (2017-05-20)
Uterine leiomyoma is the most common female reproductive tract benign tumor. Little is known about protein composition and changes in the leiomyoma interstitial fluid (IF). The present study focused on changes in protein abundance in the IF of leiomyoma. Leiomyoma
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