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Product Name
SPARC antibody
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Description
SPARC Rabbit Polyclonal antibody. Positive WB detected in human placenta tissue, A375 cells, human testis tissue. Positive IHC detected in human stomach cancer tissue. Observed molecular weight by Western-blot: 43 kDa,50 kDa
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Tested applications
ELISA, WB, IHC
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Species reactivity
Human,Mouse,Rat,Pig; other species not tested.
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Alternative names
Basement membrane protein 40 antibody; BM 40 antibody; Osteonectin antibody; SPARC antibody
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Isotype
Rabbit IgG
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Preparation
This antibody was obtained by immunization of SPARC recombinant protein (Accession Number: NM_003118). Purification method: Antigen affinity purified.
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Clonality
Polyclonal
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Formulation
PBS with 0.02% sodium azide and 50% glycerol pH 7.3.
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Storage instructions
Store at -20℃. DO NOT ALIQUOT
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Applications
Recommended Dilution:
WB: 1:1000-1:10000
IHC: 1:20-1:200
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Validations
human placenta tissue were subjected to SDS PAGE followed by western blot with Catalog No:115543(SPARC antibody) at dilution of 1:500
Immunohistochemical of paraffin-embedded human stomach cancer using Catalog No:115543(SPARC antibody) at dilution of 1:100 (under 10x lens)
Immunohistochemical of paraffin-embedded human stomach cancer using Catalog No:115543(SPARC antibody) at dilution of 1:100 (under 40x lens)
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Background
SPARC, also known as ON (Osteonectin) or BM-40 (Basement-membrane protein 40), is a 43-kDa extracellular glycoprotein that belongs to a group of matricellular proteins defined as secreted components that do not contribute directly to the formation of structural elements but serve to modulate cell-matrix interactions and cellular functions (PMID: 7542656; 12231357). SPARC is expressed at high levels in bone tissue, is distributed widely in many other tissues and cell types, and is associated generally with tissues undergoing morphogenesis, remodeling and wound repair (PMID: 10567433). It elicits changes in cell shape, inhibits cell-cycle progression, and influences the synthesis of extracellular matrix (PMID: 12721366). Altered expression of SPARC has been reported in a variety of cancers, which include breast, ovarian, colorectal, and pancreatic cancer as well as melanoma and glioblastomas (PMID: 18849185).
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References
- Loei H, Tan HT, Lim TK. Mining the gastric cancer secretome: identification of GRN as a potential diagnostic marker for early gastric cancer. Journal of proteome research. 11(3):1759-72. 2012.
- Frese KK, Neesse A, Cook N. nab-Paclitaxel potentiates gemcitabine activity by reducing cytidine deaminase levels in a mouse model of pancreatic cancer. Cancer discovery. 2(3):260-9. 2012.
- Feig C, Gopinathan A, Neesse A, Chan DS, Cook N, Tuveson DA. The pancreas cancer microenvironment. Clinical cancer research : an official journal of the American Association for Cancer Research. 18(16):4266-76. 2012.
- Kim JY, Jeong D, Ahn TS. Expression of Secreted Protein Acidic and Rich in Cysteine in the Stroma of a Colorectal Carcinoma is Associated With Patient Prognosis. Annals of coloproctology. 29(3):93-9. 2013.
- Chen SX, Xu XE, Wang XQ. Identification of colonic fibroblast secretomes reveals secretory factors regulating colon cancer cell proliferation. Journal of proteomics. 110:155-71. 2014.
- Vranka JA, Bradley JM, Yang YF, Keller KE, Acott TS. Mapping molecular differences and extracellular matrix gene expression in segmental outflow pathways of the human ocular trabecular meshwork. PloS one. 10(3):e0122483. 2015.
- Lin Q, Lim HS, Lin HL. Analysis of colorectal cancer glyco-secretome identifies laminin β-1 (LAMB1) as a potential serological biomarker for colorectal cancer. Proteomics. 15(22):3905-20. 2015.
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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"