Heat Shock Protein Cognate 4 (HSC70-4) antibody

Details for Product No. ABIN967328, Supplier: Log in to see
Antigen
  • BAP74
  • CG4264
  • Dmel\\CG4264
  • E(csp)1545
  • E(nd)195
  • HSC-70
  • HSC4
  • HSC70
  • HSC70-4
  • Hsc-4
  • Hsc4
  • Hsc4p
  • Hsc70
  • Hsp-c4
  • Hsp70
  • anon-WO0118547.237
  • bs17d06.y1
  • dhsc70
  • hsc4
  • hsc70
  • hsc70-4
  • hsp70
  • i190
  • l(3)03550
  • l(3)L3929
  • l(3)j7A4
  • scd
  • Heat shock protein cognate 4
  • Hsc70-4
Reactivity
Human
47
46
46
46
45
45
44
43
43
42
41
41
40
40
40
36
22
21
19
3
3
1
1
1
1
1
1
1
1
Host
Mouse
64
6
1
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
5
3
3
3
3
3
3
3
3
3
3
3
3
3
3
3
3
Application
Western Blotting (WB)
71
42
41
22
22
21
21
18
4
3
1
1
Options
Supplier
Log in to see
Supplier Product No.
Log in to see
Request

Get this product for free

It's quick and easy to submit your validation proposal. I want to validate this product

Learn more

Available images

Immunogen Human Hsp70/Hsc70 recombinant protein
Clone W27
Isotype IgG2a
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Please refer to us for technical protocols.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Components 1) 51-6892GR: Purified Mouse Anti-Human Hsp70/Hsc70.
Quantity: 50 µg (1 ea).
Concentration: 0.25 mg/ml.
Clone: W27.
Immunogen: Human Hsp70/Hsc70 recombinant protein.
Isotype: Mouse IgG2a.
Molecular Weight: 70 kDa.
Storage Buffer: Aqueous buffered solution containing BSA, glycerol, and Less or equal than 0.09% sodium azide.

2) 51-16516N: HeLa Control Lysate.
Quantity: 50 µg (1 ea).
Concentration: 1.0 mg/ml.
Storage Buffer: SDS-PAGE buffer (62mM Tris pH 6.8, 2% SDS, 0.9% b-mercaptoethanol, 0.003% bromophenol blue, 5% glycerol).
Alternative Name Hsp70/Hsc70
Background Heat shock proteins (Hsp70/Hsc70) are a class of proteins which increase their rate of synthesis when exposed to heat or other cellular stresses. It is now apparent that these proteins also function under normal conditions to facilitate folding and/or refolding of proteins, and to prevent aggregation. Members of the Hsp70 family bind ATP, and function as molecular chaperones by assisting in the folding of other proteins in various intracellular compartments. All Hsp70/Hsc70 proteins consist of two domains: a highly conserved N-terminal ATP-ase domain (44 kDa) and a C-terminal region (25 kDa) which is composed of a substrate binding domain.
Molecular Weight 70 kDa
Research Area Heat Shock Proteins
Comment

Related Products: ABIN968535, ABIN967389

Restrictions For Research Use only
Format Liquid
Concentration 0.25 mg/ml
Buffer Aqueous buffered solution containing BSA, glycerol.
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage -20 °C
Supplier Images
Western Blotting (WB) image for anti-Heat Shock Protein Cognate 4 (HSC70-4) antibody (ABIN967328) Western blot analysis for Hsp70/Hsc70. A HeLa cell lysate (Human cervical epitheloid ...
Product cited in: Pilon, Schekman: "Protein translocation: how Hsp70 pulls it off." in: Cell, Vol. 97, Issue 6, pp. 679-82, 1999 (PubMed).

Bukau, Horwich: "The Hsp70 and Hsp60 chaperone machines." in: Cell, Vol. 92, Issue 3, pp. 351-66, 1998 (PubMed).

Hang, Fox: "Expression of hsp70 induced in CHO cells by 45.0 degrees C hyperthermia is cell cycle associated and DNA synthesis dependent." in: Cytometry, Vol. 19, Issue 2, pp. 119-25, 1995 (PubMed).

Minota, Cameron, Welch, Winfield: "Autoantibodies to the constitutive 73-kD member of the hsp70 family of heat shock proteins in systemic lupus erythematosus." in: The Journal of experimental medicine, Vol. 168, Issue 4, pp. 1475-80, 1988 (PubMed).