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Merck
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PRS4953

Sigma-Aldrich

Anti-NIPSNAP2 (ab2) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-GBAS, Anti-Glioblastoma amplified sequence, Anti-Non-neuronal SNAP25-like protein 2

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41
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biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human, rat, mouse

technique(s)

immunohistochemistry: suitable
indirect ELISA: suitable
western blot: suitable

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GBAS(2631)

General description

NIPSNAP2 (nipsnap homolog 2) belongs to the NIPSNAP family. It is also known as GBAS (glioblastoma amplified sequence). It is located in the mitochondrial inner membrane space. It is highly expressed in skeletal muscle and heart. GBAS codes for a protein, that has tyrosine phosphorylation sites and a transmembrane domain. It is co-amplified with EGFR (epidermal growth factor receptor gene). It is located on chromosome 7p11.2.

Immunogen

a 14 amino acid peptide near the center of human NIPSNAP2.

Biochem/physiol Actions

NIPSNAP2 (nipsnap homolog 2) plays a major role in transcriptional regulation via L-type Ca2+ channels.

Physical form

Solution in phosphate buffered saline containing 0.02% sodium azide

Other Notes

The action of this antibody can be blocked using blocking peptide SBP4953.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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De novo 393 kb microdeletion of 7p11.2 characterized by aCGH in a boy with psychomotor retardation and dysmorphic features
Varvagiannis K, et al.
Meta Gene, 2, 274-282 (2014)
GBAS, a novel gene encoding a protein with tyrosine phosphorylation sites and a transmembrane domain, is co-amplified with EGFR
Wang XY, et al.
Genomics, 49(3), 448-451 (1998)
Regulation of CREB signaling through L-type Ca2+ channels by Nipsnap-2
Brittain JM, et al.
Channels (Austin, Tex.), 6(2), 94-102 (2012)
Identification of NIPSNAP1 as a nocistatin-interacting protein involving pain transmission
Okuda-Ashitaka E, et al.
The Journal of Biological Chemistry, 287(13), 10403-10413 (2012)
NIP-SNAP-1 and -2 mitochondrial proteins are maintained by heat shock protein 60
Yamamoto S, et al.
Biochemical and Biophysical Research Communications, 483(3), 917-922 (2017)

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