HSPA5[30028]

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Western blot analysis using HSPA5 mouse mAb against NIH/3T3 (1), Hela (2) and Jurkat (3) cell lysate.

Immunohistochemical analysis of paraffin-embedded human Thyroid tissues using HSPA5 mouse mAb

Mouse Monoclonal Antibody to HSPA5

货号：
30028
别名：
BIP; MIF2; GRP78; FLJ26106; HSPA5
应用：
WB,IHC
反应种属：
Human
规格：

100μl
50μl
数量：

-

+
说明书：

目录价¥2180

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Mouse Monoclonal Antibody to HSPA5

Description
When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) (PubMed 8020977) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell.Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.The HSP70 proteins are ubiquitous molecular chaparones that are found in all organisms and tissue types. Like other members of the HSP70 family, BiP is a peptide-binding ATPase that is able to differentiate native proteins from unfolded polypeptides. BiP does not bind to fully folded and assembled proteins, except in the presence of other co-chaparones. BiP is involved in a number of key mechanisms and pathways including polypeptide translocation across the endoplasmic reticulum, folding, assembly, transport of secreted or membrane proteins, and the regulation of calcium homeostasis. Although BiP is relatively abundant, marked increases in BiP occur where there is an accumulation of unfolded polypeptides. For this reason, BiP has been identified as a marker for various disease states that are associated with secretory and transmembrane protein misfolding.

Description

When Chinese hamster K12 cells are starved of glucose, the synthesis of several proteins, called glucose-regulated proteins (GRPs), is markedly increased. Hendershot et al. (1994) (PubMed 8020977) pointed out that one of these, GRP78 (HSPA5), also referred to as 'immunoglobulin heavy chain-binding protein' (BiP), is a member of the heat-shock protein-70 (HSP70) family and is involved in the folding and assembly of proteins in the endoplasmic reticulum (ER). Because so many ER proteins interact transiently with GRP78, it may play a key role in monitoring protein transport through the cell.Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.The HSP70 proteins are ubiquitous molecular chaparones that are found in all organisms and tissue types. Like other members of the HSP70 family, BiP is a peptide-binding ATPase that is able to differentiate native proteins from unfolded polypeptides. BiP does not bind to fully folded and assembled proteins, except in the presence of other co-chaparones. BiP is involved in a number of key mechanisms and pathways including polypeptide translocation across the endoplasmic reticulum, folding, assembly, transport of secreted or membrane proteins, and the regulation of calcium homeostasis. Although BiP is relatively abundant, marked increases in BiP occur where there is an accumulation of unfolded polypeptides. For this reason, BiP has been identified as a marker for various disease states that are associated with secretory and transmembrane protein misfolding.

References
1. Int J Cancer. 2010 Apr 1;126(7):1562-9. 2. J Virol. 2009 Dec;83(23):12622-5. 3. Mod Pathol. 2010 Jan;23(1):45-53.

Specification
Aliases	BIP; MIF2; GRP78; FLJ26106; HSPA5
Entrez GeneID	3309
Swissprot	P11021
clone	4E3
WB Predicted band size	78kDa
Host/Isotype	Mouse IgG1
Antibody Type	Primary antibody
Storage	Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze/thaw cycles.
Species Reactivity	Human
Immunogen	Purified recombinant fragment of human HSPA5 expressed in E. Coli.
Formulation	Ascitic fluid containing 0.03% sodium azide.