Recombinant HSPH1 antibody (C-Term)

Catalog No. ABIN8093227

This Mouse Monoclonal antibody specifically detects HSPH1 in WB and IHC. It exhibits reactivity toward Human.

Quick Overview for Recombinant HSPH1 antibody (C-Term) (ABIN8093227)

Target: HSPH1 (Heat Shock 105kDa/110kDa Protein 1 (HSPH1))

Antibody Type: Recombinant Antibody

Reactivity: Human

Host: Mouse

Clonality: Monoclonal

Conjugate: This HSPH1 antibody is un-conjugated

Application: Western Blotting (WB), Immunohistochemistry (IHC)

Grade: Carrier-free

Clone: R58F12

Product Details anti-HSPH1 Antibody

Binding Specificity: C-Term

Purpose: HSPH1 Antibody / Heat shock protein 105 kDa (azide and preservative free)

Immunogen: Prokaryotic recombinant protein of 31 kD corresponding to the C-terminus of the heat shock protein 105 molecule was used as the immunogen for the HSPH1/Heat shock protein 105 kDa antibody.

Isotype: IgG1, kappa

Application Details

Application Notes: 1. Optimal dilution of the HSPH1/Heat shock protein 105 kDa antibody should be determined by the researcher.

2. This HSPH1/Heat shock protein 105 kDa antibody is recombinantly produced by expression in CHO cells.

Restrictions: For Research Use only

Handling

Format: Liquid

Concentration: 1 mg/mL

Buffer: 1 mg/mL in 1X PBS, BSA free, sodium azide free

Preservative: Azide free

Storage: -20 °C,-80 °C

Storage Comment: HSPH1/Heat shock protein 105 kDa antibody with sodium azide - store at 2 to 8oC, antibody without sodium azide - store at -20 to -80oC.

Target Details for HSPH1

Target: HSPH1 (Heat Shock 105kDa/110kDa Protein 1 (HSPH1))

Alternative Name: HSPH1

Background: HSPH1 antibody is used to study Heat shock protein 105 kDa, a molecular chaperone involved in cellular stress responses and protein homeostasis. Heat shock protein 105 kDa is encoded by the HSPH1 gene and belongs to the HSP110 family of heat shock proteins, which function as nucleotide exchange factors for HSP70 chaperones. Through this activity, Heat shock protein 105 kDa supports protein folding, prevents aggregation of misfolded proteins, and helps maintain proteostasis under conditions of cellular stress.

Heat shock protein 105 kDa is also commonly referred to as HSP105 or HSP110 in the literature, reflecting its classification within the high-molecular-weight heat shock protein family. Unlike smaller heat shock proteins, HSPH1 exhibits strong ATP-dependent chaperone activity and plays an important role in stabilizing denatured proteins during heat shock and other stress conditions. Use of an HSPH1 antibody enables investigation of these stress-responsive chaperone functions in cell and tissue-based research models.

At the subcellular level, Heat shock protein 105 kDa localizes primarily to the cytoplasm, where it associates with protein complexes involved in folding and quality control. Under stress conditions, redistribution of HSPH1 has been reported, reflecting dynamic engagement with unfolded protein substrates. Studies using HSPH1 antibody have contributed to understanding how cells adapt to environmental stressors and maintain protein integrity through coordinated chaperone networks.

Altered expression of Heat shock protein 105 kDa has been examined in cancer biology and stress adaptation studies, where increased HSPH1 levels are often associated with enhanced cellular survival under proteotoxic stress. In tumor-derived cells, elevated HSPH1 expression is thought to support malignant growth by buffering protein-folding stress and stabilizing oncogenic signaling proteins. Detection of HSPH1 using an HSPH1 antibody supports research into stress tolerance, protein quality control, and cellular adaptation mechanisms in disease-associated contexts.

HSPH1 antibody (clone r58F12) is designed to detect Heat shock protein 105 kDa in research applications. Analysis of HSPH1 expression provides insight into chaperone-mediated protein folding, stress response pathways, and proteostasis regulation. Heat shock protein 105 kDa remains a key component of cellular defense mechanisms that protect against protein misfolding and stress-induced damage.

UniProt: Q92598