HSP70-1A (HSPA1A) Mouse Monoclonal Antibody [Clone ID: SJ-70]

Specifications

Product Data
Clone Name	SJ-70
Applications	IF, IHC, IP, WB
Recommend Dilution	Western Blot: 0.5 μg/ml. Immunohistochemistry on frozen and paraffin sections: 0.5 - 1 μg/ml.
Reactivity	Human
Host	Mouse
Clonality	Monoclonal
Immunogen	HSP70 isolated from bovine brain
Specificity	This antibody reacts to Heat shock protein 70.
Formulation	1.2 % sodium acetate, with 2 mg BSA and 0.01 mg sodium azide as preservative. State: Purified State: Lyphilized purified Ig fraction
Reconstitution Method	Restore with 1.2% sodium acetate or neutral PBS
Concentration	0,1 mg/ml (after reconstitution with PBS)
Purification	Affinity chromatography
Conjugation	Unconjugated
Storage Condition	Prior to reconstitution store at -20°C. Following reconstitution store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing.
Gene Name	heat shock protein family A (Hsp70) member 1A
Database Link	Entrez Gene 3303 Human UniProt ID P0DMV8
Background	Heat-shock proteins, or stress proteins, are expressed in response to heat shock and a variety of other stress stimuli including oxidative free radicals and toxic metal ions. Sargent et al. (1989) identified a duplicated HSP70 locus in the class III region of the major histocompatibility complex on 6p21.3. A duplicated locus encoding the major heat shock-induced protein HSP70 is located in the major histocompatibility complex (MHC) class III region 92 kilobases (kb) telomeric to the C2 gene. The 70-kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles.The 70 kilodalton heat shock proteins (Hsp70s) are a family of ubiquitously expressed heat shock proteins. The Hsp70s are an important part of the cell's machinery for protein folding, and help to protect cells from stress. All of the Hsp70 proteins have three major functional domains: An N-terminal ATPase domain binds ATP (Adenosine triphosphate) and hydrolyzes it to ADP (Adenosine diphosphate); A substrate binding domain contains a groove with an affinity for neutral, hydrophobic amino acid residues; A C-terminal domain rich in alpha helical structure acts as a 'lid' for the substrate binding domain. By binding tightly to partially-synthesized peptide sequences (incomplete proteins),Hsp70 prevents them from aggregating and being rendered nonfunctional. And it also can act to protect cells from thermal or oxidative stress. Finally, Hsp70 seems to be able to participate in disposal of damaged or defective proteins. Interaction with CHIP (Carboxyl-terminus of Hsp70 Interacting Protein)–an E3 ubiquitin ligase–allows Hsp70 to pass proteins to the cell's ubiquitination and proteolysis pathways.
Synonyms	HSP70.1, HSP70-1/HSP70-2, HSPA1A, HSPA1B, HSPA1
Reference Data
Protein Pathways	Antigen processing and presentation, Endocytosis, MAPK signaling pathway, Prion diseases, Spliceosome

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