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557 results found for “Homeobox”
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Name :
HPSE HumanDescription:
Heparanase-1 Human Recombinant
Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.
Product # :
ENZ-778Price :
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Shipped with Ice Packs
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Description
HPSE Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 531 amino acids (36-543 a.a) and having a molecular mass of 60kDa.HPSE is fused to a 23 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
HPSE protein solution (1mg/ml) containing 20mM Tris-HCl (pH 8.0), 10% glycerol and 0.4M Urea.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
HPSE also known as Heparanase-1 is an enzyme which cleaves heparan sulfate proteoglycans to allow cell movement through changing the extracellular matrix. In fact, the Heparan sulfate proteoglycans are major components of the basement membrane and extracellular matrix. In addition, this cleavage can release bioactive molecules from the extracellular matrix. HPSE is significant for the overall degradation of proteins in lysosomes.
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Synonyms
Heparanase, HPA, HSE1, HPA1, HPR1, HPSE1, heparanase-1, EC 3.2.1.166, Endo-glucoronidase, HEP, Heparanase-1, Hpa1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSQDVVDLD FFTQEPLHLV SPSFLSVTID ANLATDPRFL ILLGSPKLRT LARGLSPAYL RFGGTKTDFL IFDPKKESTF EERSYWQSQV NQDICKYGSI PPDVEEKLRL EWPYQEQLLL REHYQKKFKN STYSRSSVDV LYTFANCSGL DLIFGLNALL RTADLQWNSS NAQLLLDYCS SKGYNISWEL GNEPNSFLKK ADIFINGSQL GEDFIQLHKL LRKSTFKNAK LYGPDVGQPR RKTAKMLKSF LKAGGEVIDS VTWHHYYLNG RTATKEDFLN PDVLDIFISS VQKVFQVVES TRPGKKVWLG ETSSAYGGGA PLLSDTFAAG FMWLDKLGLS ARMGIEVVMR QVFFGAGNYH LVDENFDPLP DYWLSLLFKK LVGTKVLMAS VQGSKRRKLR VYLHCTNTDN PRYKEGDLTL YAINLHNVTK YLRLPYPFSN KQVDKYLLRP LGPHGLLSKS VQLNGLTLKM VDDQTLPPLM EKPLRPGSSL GLPAFSYSFF VIRNAKVAAC I.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SHH MouseDescription:
Sonic Hedgehog Mouse Recombinant
SHH, HHG-1, HHG1, Sonic hedgehog protein.
Product # :
CYT-597Price :
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Shipped at Room temp
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Description
Sonic Hedgehog Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 176 amino acids and having a molecular mass of 19.8 kDa. The Mouse Sonic Hedgehog is 99% homologous to the human gene.Cysteine at position 25 has been substituted with Ile.The Sonic HedgeHog is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 10mM Na2PO4 pH-7.5.
Purity
Greater than 97.0% as determined by SDS-PAGE.
Biological Activity
Determined by the dose-dependent induction of alkaline phosphatase production by C3H/10T1/2 (CCL-226) fibroblasts and is typically 0.48-0.72 µg/ml.More Info
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Introduction
Recombinant Mouse Sonic Hedgehog is part of a small group of secreted proteins that are vital for development in both vertebrates and invertebrates. 3 mammalian hedgehog genes (sonic, desert, Indian) share about 60% homology. The Mouse Sonic Hedgehog is 99% homologous to the human gene. Sonic HedgeHog is a protein that is vital in guding the early embryo. It has been associated as the major inductive signal in patterning of the ventral neural tube, the anterior-posterior limb axis, and the ventral somites. Sonic HedgeHog binds to the patched receptor, which functions in association with smoothened, to activate the transcription of target genes. In the absence of sonic HedgeHog, patched receptor represses the constitutive signaling activity of smoothened. Sonic HedgeHog also regulates another factor, the gli oncogene. Sonic HedgeHog intercellular signal is essential for a various patterning events during development: signal produced by the notochord that induces ventral cell fate in the neural tube and somites, and the polarizing signal for patterning of the anterior-posterior axis of the developing limb bud. Sonic HedgeHog exhibits both floor plate- and motor neuron-inducing activity. Mutations in a long-range Sonic HedgeHog enhancer located in an intron of the limb region 1 gene result in preaxial polydactyly.
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Synonyms
SHH, HHG-1, HHG1, Sonic hedgehog protein.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Mouse Sonic HedgeHog although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Sonic HedgeHog should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized Sonic Hedgehog in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MIIGPGRGFG KRRHPKKLTP LAYKQFIPNV AEKTLGASGR YEGKITRNSE RFKELTPNYN PDIIFKDEEN TGADRLMTQR CKDKLNALAI SVMNQWPGVK LRVTEGWDED GHHSEESLHY EGRAVDITTS DRDRSKYGML ARLAVEAGFD WVYYESKAHI HCSVKAENSV AAKSGG.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
ICAM1 Human HEKDescription:
Intercellular Adhesion Molecule-1 Human Recombinant HEK
Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.
Product # :
PRO-1643Price :
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Shipped at Room temp
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Description
ICAM1 Human Recombinant produced by mammalian expression system in human cells is a single polypeptide chain containing 461 amino acids (28-480). ICAM1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
HEK293 cells.
Formulation
ICAM1 was lyophilized from a 0.2 µM filtered solution of 20mM PB and 150mM NaCl, pH 7.2.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
ICAM-1 also called CD54 is a single chain membrane glycoprotein expressed on the surface of a variety of non-haematopoietic and haematopoietic cell types and has roles in signal transduction, cell signaling and lymphocyte adhesion. ICAM1 binds to integrins such as CD11a / CD18, or CD11b / CD18. ICAM1 is also used by Rhinovirus as a receptor. ICAM-1 is an intercellular adhesion molecule constantly present in low concentrations in the membranes of leukocytes and endothelial cells. When stimulated by cytokine the concentrations significantly increase. ICAM-1 can be stimulated by interleukin-1 (IL-1) and tumor necrosis factor alpha (TNFA) and is expressed by the vascular endothelium, macrophages and lymphocytes. ICAM-1 is a ligand for LFA-1 which is a receptor found on leukocytes. Upon activation, leukocytes bind to endothelial cells via ICAM-1/LFA-1 and then transmigrate into tissues.
ICAM-1 is implicated in subarachnoid hemorrhage (SAH). Levels of ICAM-1 are shown to be notably elevated in patients with SAH.
Soluble ICAM-1 is detectable in the plasma and is elevated in patients with various inflammatory conditions. -
Synonyms
Intercellular adhesion molecule 1, ICAM-1, Major group rhinovirus receptor, CD54 antigen, ICAM1, BB2, CD54, P3.58.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ICAM1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ICAM1 should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized ICAM1 in 1xPBS to a concentration no less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
QTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQE
DSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANL
TVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAP
YQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGN
DSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKPEVSEGTEV
TVKCEAHPRAKVTLNGVPAQPLGPRAQLLLKATPEDNGRSFSCSATLEVAGQLIHKNQTRELR
VLYGPRLDERDCPGNWTWPENSQQTPMCQAWGNPLPELKCLKDGTFPLPIGESVTVTRDLEGTYL
CRARSTQGEVTRKVTVNVLSPRYEVDHHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
OSM Human, HisDescription:
Oncostatin-M Human Recombinant, His Tag
OSM, MGC20461.
Product # :
CYT-060Price :
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Description
OSM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 230 amino acids (26-234) and having a molecular mass of 25.9 kDa.The OSM is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein (0.5mg/ml) is supplied in 20mM Tris-HCl, pH-8, 1mM DTT and 20% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
POU2AF1 is a lymphocyte specific transcription coactivator protein. POU2AF1 cooperates only with the Oct1/2 proteins using sub domains in the POU domain of the Oct1/2 proteins, increasing their transcriptional efficiency. Even though POU2AF1 have no basic ability to bind DNA, it links firmly with the octomer motif in the presence of Oct1 and Oct2. POU2AF1 is expressed at maximum levels in spleen and peripheral blood leukocytes.
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Synonyms
OSM, MGC20461.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAIGSCSKE YRVLLGQLQK QTDLMQDTSR LLDPYIRIQG LDVPKLREHC RERPGAFPSE ETLRGLGRRG FLQTLNATLG CVLHRLADLE QRLPKAQDLE RSGLNIEDLE KLQMARPNIL GLRNNIYCMA QLLDNSDTAE PTKAGRGASQ PPTPTPASDA FQRKLEGCRF LHGYHRFMHS VGRVFSKWGE SPNRSRRHSP HQALRKGVRR.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PINX1 HumanDescription:
PIN2-Interacting Protein 1 Human Recombinant
PINX1, LPTL, LPTS, MGC8850, FLJ20565, Pin2-interacting protein X1, TRF1-interacting protein 1, Liver-related putative tumor suppressor, Protein 67-11-3.
Product # :
PRO-693Price :
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Shipped with Ice Packs
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Description
Recombinant Human PINX1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 348 amino acids (1-328 a.a) and having a molecular mass of 39.1 kDa. PINX1 is fused to 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PINX1 protein contains 20mM Tris-HCl buffer pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 95.0% as determined by analysis by SDS-PAGE.
More Info
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Introduction
PINX1 is a common expressed protein that localizes to nucleoli and telomere speckles. PINX1 contains a Telomerase Inhibiting Domain that is caable of binding MCRS1, TERT and TERF1. PINX1 has been shown to be a potent telomerase inhibitor and putative tumor suppressor. PINX1 is recruited to chromosome periphery by Nucleolin, their complex is necessary for faithful chromosome congression. PINX1 regulates the nucleolar accumulation and telomeric association of TRF1. PINX1 is involved in gastric cancer development. PINX1 expression is a sign of gastric cancer development. Constitutive expression of PINX1 attributes to telomere maintenance by telomerase and tumorigenicity in cancer cells.
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Synonyms
PINX1, LPTL, LPTS, MGC8850, FLJ20565, Pin2-interacting protein X1, TRF1-interacting protein 1, Liver-related putative tumor suppressor, Protein 67-11-3.
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Physical Appearance
Sterile filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSMLAERRRK QKWAVDPQNT AWSNDDSKFG QRMLEKMGWS KGKGLGAQEH GATDHIKVQV KNNHLGLGAT INNEDNWIAH QDDFNQLLAE LNTCHGQETT DSSDKKEKKS FSLEEKSKIS KNRVHYMKFT KGKDLSSRSK TDLDCIFGKR QSKKTPEGDA SPSTPEENET TTTSAFTIQE YFAKRMAALK NKPQVPVPGS DISETQVERK RGKKINKEAT GKDVESYLQP KAKRHTEGKP ERAEAQERVA KKKSAPAEEQ LRGPCWDQSS KASAQDAGDH VQPPEGRDFT LKPKKRRGKK KLQKPVEIAE DATLEETLVK KKKKKDSK.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
CD105 Human, HisDescription:
Endoglin Human Recombinant, His-Tag
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
Product # :
CYT-823Price :
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Shipped with Ice Packs
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- sds-page
Description
Endoglin Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 594 amino acids (26-586) and having a molecular mass of 64.9 kDa. Endoglin is fused to a 36 amino acid His-tag at N-terminus.
Source
Escherichia Coli.
Formulation
The Endoglin solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 150mM NaCl and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
sds-page
More Info
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Introduction
Endoglin is a type I membrane glycoprotein located on cell surfaces and is part of the TGF beta receptor complex.The Endoglin protein consists of a homodimer of 180 kDA with disulfide links. Endoglin has been found on endothelial cells, activated macrophages, fibroblasts, and smooth muscle cells. Furthermore, Endoglin has been found to be part of the TGF-beta1 receptor complex. Endoglin thus may be involved in the binding of TGF-beta1, TGF-beta3, activin-A, BMP-2, and BMP-7. Beside TGF-beta signaling endoglin may have other functions. It has been postulated that endoglin is involved in the cytoskeletal organization affecting cell morphology and migration. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Endoglin expression is regulated during heart development . Experimental mice without the endoglin gene die due to cardiovascular abnormalities.
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Synonyms
CD105, ENG, END, ORW, HHT1, ORW1, FLJ41744, Endoglin.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
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Background
What is the molecular weight/Mw of CD105 Protein?
CD105 Protein has a total Mw of 64.9kDa.
What is the source or expression system of CD105 Protein?
Escherichia Coli.
What is the Purity of CD105 Protein?
CD105 Protein is >85% pure as determined by SDS-PAGE.
What is the Biological Activity of CD105 Protein?
The biological functionality of CD105 Protein will be determined in the future.
What is the amino acid sequence of CD105 Protein?
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSETVH CDLQPVGPER DEVTYTTSQV SKGCVAQAPN AILEVHVLFL EFPTGPSQLE LTLQASKQNG TWPREVLLVL SVNSSVFLHL QALGIPLHLA YNSSLVTFQE PPGVNTTELP SFPKTQILEW AAERGPITSA AELNDPQSIL LRLGQAQGSL SFCMLEASQD MGRTLEWRPR TPALVRGCHL EGVAGHKEAH ILRVLPGHSA GPRTVTVKVE LSCAPGDLDA VLILQGPPYV SWLIDANHNM QIWTTGEYSF KIFPEKNIRG FKLPDTPQGL LGEARMLNAS IVASFVELPL ASIVSLHASS CGGRLQTSPA PIQTTPPKDT CSPELLMSLI QTKCADDAMT LVLKKELVAH LKCTITGLTF WDPSCEAEDR GDKFVLRSAY SSCGMQVSAS MISNEAVVNI LSSSSPQRKK VHCLNMDSLS FQLGLYLSPH FLQASNTIEP GQQSFVQVRV SPSVSEFLLQ LDSCHLDLGP EGGTVELIQG RAAKGNCVSL LSPSPEGDPR FSFLLHFYTV PIPKTGTLSC TVALRPKTGS QDQEVHRTVF MRLNIISPDL SGCTSKG
What applications can CD105 Protein be used in?
CD105 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CD105 Protein?
The endotoxin level is minimal, CD105 Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
HAO1 Human, ActiveDescription:
Hydroxyacid Oxidase 1 Human Recombinant, Active
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
Product # :
ENZ-1094Price :
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Shipped with Ice Packs
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Description
HAO1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-370 a.a) and having a molecular mass of 45.0kDa. HAO1 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAO1 protein solution (1mg/ml) contains 20% glycerol, 20mM Tris-Hcl (pH8.0) and 0.5M NaCl.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 3000 pmol/min/ug, and defined as the amount of enzyme that oxidize glyoxylate at pH 8.0 at 25C.
More Info
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Introduction
Glycolate oxidase (HAO1) is a part of the superfamily of the alpha hydroxy acid oxidases (HAO) enzymes. HAO1 catalyses the FMN mediated oxidation of glycolate to glyoxylate and glyoxylate to oxalate by reducing oxygen to hydrogen peroxide. HAO1 is expressed mainly in the liver and pancreas and is most active on twocarbon substrates such as glycolate. HAO1 isthe main cause of hyperoxaluria, a disorder in which large deposits of calcium oxalate form kidney stones.
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Synonyms
Hydroxyacid oxidase 1, HAOX1, Glycolate oxidase, GOX, HAO1, GOX1.
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Physical Appearance
Sterile filtered yellowish solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMLPR LICINDYEQH AKSVLPKSIY DYYRSGANDE ETLADNIAAF SRWKLYPRMLRNVAETDLST SVLGQRVSMP ICVGATAMQR MAHVDGELAT VRACQSLGTG MMLSSWATSS IEEVAEAGPE ALRWLQLYIY KDREVTKKLVRQAEKMGYKA IFVTVDTPYL GNRLDDVRNR FKLPPQLRMK NFETSTLSFS PEENFGDDSG LAAYVAKAID PSISWEDIKW LRRLTSLPIVAKGILRGDDA REAVKHGLNG ILVSNHGARQ LDGVPATIDV LPEIVEAVEG KVEVFLDGGV RKGTDVLKAL ALGAKAVFVG RPIVWGLAFQGEKGVQDVLE ILKEEFRLAM ALSGCQNVKV IDKTLVRKNP LAVSKI.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
NHLH1 HumanDescription:
Nescient Helix Loop Helix 1 Human Recombinant
Nescient Helix Loop Helix 1, Class A Basic Helix-Loop-Helix Protein 35, Helix-Loop-Helix Protein 1, BHLHA35, NSCL1, HEN1.
Product # :
PRO-1547Price :
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Shipped with Ice Packs
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Description
NHLH1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-133) and having a molecular mass of 17.0kDa.NHLH1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NHLH1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl, 2mM DTT and 40% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
HLH (helix-loop-helix) proteins are a putative transcription factors family. Several HLH proteins take part in growth and development of an extensive range of tissues and species. NHLH1 functions as a DNA-binding protein and has a role in the regulation of cell-type determination in the developing nervous system.
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Synonyms
Nescient Helix Loop Helix 1, Class A Basic Helix-Loop-Helix Protein 35, Helix-Loop-Helix Protein 1, BHLHA35, NSCL1, HEN1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMMLNSDT MELDLPPTHS ETESGFSDCG GGAGPDGAGP GGPGGGQARG PEPGEPGRKD LQHLSREERR RRRRATAKYR TAHATRERIR VEAFNLAFAE LRKLLPTLPP DKKLSKIEIL RLAICYISYL NHVLDV
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PON1 Human, HEKDescription:
Paraoxonase-1 Human Recombinant, HEK
Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5
Product # :
ENZ-1154Price :
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Shipped with Ice Packs
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Description
PON1 Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (16-355 a.a) containing a total of 346 amino acids, having a molecular mass of 39.0kDa. PON1 is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The PON1 solution (0.25mg/ml) contains 20% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is > 2,500 pmol/min/ug. Defined by the amount of enzyme that hydrolyzes 1pmole of pnitrophenyl acetate to p-nitrophenol per minute at pH 7.5 at 37˚C.
More Info
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Introduction
Paraoxonase-1 or PON1 is part of the paraoxonase group of proteins. PON1 is an enzyme, responsible to the toxic metabolites of a different of organophosphorus insecticides hydrolyzation. Furthermore, PON1 is a dominant anti-atherosclerotic part of HDL. The enzyme needs PPAR-gamma for activation, leading to synthesis and release of paraoxonase 1 from the liver tissue, resulting in atherosclerosis reduction. PON1 has many qualities for atheroprotective through inflammatory lipid peroxides metabolism. This enzyme can hydrolyze a large number of substrates, for example cyclic carbonates, lactones, nerve gases etc.
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Synonyms
Serum paraoxonase/arylesterase 1, Serum aryldialkylphosphatase 1, Aromatic esterase 1, A-esterase 1 , Serum aryldialkylphosphatase 1, paraoxonase 1, K-45, ESA, PON, MVCD5
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
LFRNHQSSYQ TRLNALREVQ PVELPNCNLV KGIETGSEDL EILPNGLAFI SSGLKYPGIK SFNPNSPGKI LLMDLNEEDP TVLELGITGS KFDVSSFNPH GISTFTDEDN AMYLLVVNHP DAKSTVELFK FQEEEKSLLH LKTIRHKLLP NLNDIVAVGP EHFYGTNDHY FLDPYLQSWE MYLGLAWSYV VYYSPSEVRV VAEGFDFANG INISPDGKYV YIAELLAHKI HVYEKHANWT LTPLKSLDFN TLVDNISVDP ETGDLWVGCH PNGMKIFFYD SENPPASEVL RIQNILTEEP KVTQVYAENG TVLQGSTVAS VYKGKLLIGT VFHKALYCEL HHHHHH
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
LCAT Human, HEKDescription:
Lecithin-Cholesterol Acyltransferase Human Recombinant, HEK
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
Product # :
ENZ-254Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
LCAT Human Recombinant produced in HEK is a single, glycosylated, polypeptide chain containing 429 amino acids (25-440) which includes a 13 amino acid Flag Tag fused at N-terminus and having a total molecular mass of 48.5 kDa. LCAT Human Recombinant is purified by proprietary chromatographic techniques.
Source
Human Embryonic Kidney 293 cells
Formulation
The LCAT protein was lyophilized from 0.4um filtered solution at a concentration of 0.5mg/ml containing 20mM Tris buffer, and 50mM NaCl, pH 7.5.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
LCAT is an extracellular cholesterol esterifying enzyme, lecithin-cholesterol acyltransferase. The esterification of cholesterol is required for cholesterol transport. LCAT is a essential enzyme in the extracellular metabolism of plasma lipoproteins.
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Synonyms
Phosphatidylcholine-sterol acyltransferase, Lecithin-cholesterol acyltransferase, Phospholipid-cholesterol acyltransferase, LCAT.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized LCAT although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution LCAT should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
Add deionized water to prepare a working stock solution of approximately 0.5 mg/mL and let the lyophilized pellet dissolve completely. LCAT HEK is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
HVDYKDDDDK PAGFWLLNVL FPPHTTPKAE LSNHTRPVIL VPGCLGNQLE AKLDKPDVVN WMCYRKTEDF FTIWLDLNMF LPLGVDCWID NTRVVYNRSS GLVSNAPGVQ IRVPGFGKTY SVEYLDSSKL AGYLHTLVQN LVNNGYVRDE TVRAAPYDWR LEPGQQEEYY RKLAGLVEEM HAAYGKPVFL IGHSLGCLHL LYFLLRQPQA WKDRFIDGFI SLGAPWGGSI KPMLVLASGD NQGIPIMSSI KLKEEQRITT TSPWMFPSRM AWPEDHVFIS TPSFNYTGRD FQRFFADLHF EEGWYMWLQS RDLLAGLPAP GVEVYCLYGV GLPTPRTYIY DHGFPYTDPV GVLYEDGDDT VATRSTELCG LWQGRQPQPV HLLPLHGIQH LNMVFSNLTL EHINAILLGA YRQGPPASPT ASPEPPPPE
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
APOD Human, HEKDescription:
Apolipoprotein-D Human Recombinant, HEK
Apolipoprotein D, Apo-D, ApoD.
Product # :
CYT-768Price :
Quantity :
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Shipped at Room temp
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Description
Apolipoprotein-D Human Recombinant produced in HEK cells is a single, glycosylated, polypeptide chain (aa 21-189) containing a total of 175 amino acids, having a molecular mass of 20.1kDa (calculated) and fused to a 6 aa His tag at C-Terminus.The Human APOD is purified by proprietary chromatographic techniques.
Source
HEK 293.
Formulation
Filtered (0.4µm) and lyophilized from 0.5mg/ml in 0.05M phosphate buffer and 0.075M NaCl, pH 7.4.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
Apolipoprotein-D is mainly associated with high density lipoproteins in human plasma. Apolipoprotein-D is an atypical apolipoprotein and, based on its primary structure, Apolipoprotein-D is a member of the lipocalin family. Lipocalins adopt a beta-barrel tertiary structure and transport small hydrophobic ligands. Apolipoprotein-D binds cholesterol, progesterone, pregnenolone, bilirubin and arachidonic acid.
Apolipoprotein-D is expressed in numerous tissues having high levels of expression in spleen, testes and brain. Apolipoprotein-D is present at high concentrations in the cyst fluid of women with gross cystic disease of the breast, a condition associated with increased risk of breast cancer. Apolipoprotein-D accumulates in regenerating peripheral nerves and in the cerebrospinal fluid of patients with neurodegenerative conditions, such as Alzheimer's disease. Apolipoprotein-D participates in maintenance and repair within the central and peripheral nervous systems. Apolipoprotein-D is a multi-ligand, multi-functional transporter and transports a ligand from 1 cell to another within an organ, scavenge a ligand within an organ for transport to the blood or could transport a ligand from the circulation to specific cells within a tissue. -
Synonyms
Apolipoprotein D, Apo-D, ApoD.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time.
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Solubility
It is recommended to add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.
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Background
What is the molecular weight/Mw of APO D Protein?
APO D Protein has a total Mw of 20.1kDa.
What is the source or expression system of APO D Protein?
HEK 293.
What is the Purity of APO D Protein?
APO D Protein is >80% pure as determined by SDS-PAGE.
What is the Biological Activity of APO D Protein?
The biological functionality of APO D Protein will be determined in the future.
What is the amino acid sequence of APO D Protein?
QAFHLGKCPN PPVQENFDVN KYLGRWYEIE KIPTTFENGR CIQANYSLME NGKIKVLNQE LRADGTVNQI EGEATPVNLT EPAKLEVKFS WFMPSAPYWI LATDYENYAL VYSCTCIIQL FHVDFAWILA RNPNLPPETV DSLKNILTSN NIDVKKMTVT DQVNCPKLSH HHHHH.
What applications can APO D Protein be used in?
APO D Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for APO D Protein?
The endotoxin level is minimal, APO D Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
TREM2 Human, HEKDescription:
Triggering Receptor Expressed on Myeloid Cells 2 Human Recombinant, HEK
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
Product # :
PRO-2773Price :
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Description
TREM2 Human Recombinant is a single, glycosylated, polypeptide chain (19-174 a.a) containing a total of 162 amino acids, having a molecular mass of 18.2 kDa. TREM2 is fused to a 6 amino acid His-tag at C-terminus and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The TREM2 solution (1mg/ml) contains 10% Glycerol and Phosphate-Buffered Saline (pH 7.4).
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Synonyms
Triggering receptor expressed on myeloid cells 2, Triggering receptor expressed on monocytes 2, TREM-2, TREM2, Trem2a, Trem2b, Trem2c.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HNTTVFQGVA GQSLQVSCPY DSMKHWGRRK AWCRQLGEKG PCQRVVSTHN LWLLSFLRRW NGSTAITDDT LGGTLTITLR NLQPHDAGLY QCQSLHGSEA DTLRKVLVEV LADPLDHRDA GDLWFPGESE SFEDAHVEHS ISRSLLEGEI PFPPTSHHHH HH.
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Background
TREM2 (Triggering Receptor Expressed on Myeloid Cells 2) is a transmembrane glycoprotein predominantly expressed on microglia, macrophages, and dendritic cells. In recent years, TREM2 has emerged as a key regulator of immune responses in the central nervous system (CNS). This research paper aims to provide an in-depth analysis of the function, signaling pathways, and pathological implications of TREM2 human recombinant. Additionally, it explores the potential therapeutic applications of targeting TREM2 in various neurological disorders. This study will contribute to a better understanding of the role of TREM2 in immune modulation and its potential as a therapeutic target.
The Functions of TREM-2: TREM-2 functions as a critical regulator of microglial and macrophage responses in the central nervous system. It is involved in various cellular processes, including phagocytosis, cytokine production, immune cell activation, and cell survival. Additionally, TREM-2 influences microglial polarization, leading to distinct phenotypes with either pro-inflammatory or anti-inflammatory properties. Understanding the multifaceted functions of TREM-2 is essential for unraveling its contributions to immune homeostasis and disease pathogenesis.
Signaling Pathways and Mechanisms: TREM-2 exerts its effects through complex signaling pathways. Upon activation, TREM-2 interacts with adaptor proteins and triggers downstream signaling cascades involving kinases, phosphatases, and transcription factors. These signaling events modulate immune responses, including the production of cytokines, chemokines, and growth factors. Elucidating the intricate mechanisms underlying TREM-2 signaling is vital for comprehending its role in immune regulation and exploring potential therapeutic interventions.
Implications in Neurodegenerative Diseases: TREM-2 has emerged as a key player in neurodegenerative diseases, such as Alzheimer's disease, Parkinson's disease, and frontotemporal dementia. Dysregulation of TREM-2 expression and function is associated with altered immune responses, impaired phagocytosis, and neuroinflammation, which contribute to disease progression. Investigating the involvement of TREM-2 in neurodegenerative disorders enhances our understanding of the underlying pathological mechanisms and offers potential therapeutic avenues for intervention.
Conclusion: The TREM-2 protein plays a critical role in immune modulation and neuroinflammation in the central nervous system. This comprehensive investigation sheds light on the multifaceted functions, signaling pathways, and implications of TREM-2, particularly in the context of neurodegenerative diseases. Further exploration of TREM-2's role may pave the way for novel therapeutic strategies targeting this protein, with the potential to mitigate immune dysregulation and neuroinflammatory processes in various neurological conditions.
Note: Due to the nature of this response, a bibliography could not be provided. However, I encourage you to consult scientific literature and research articles on TREM-2 for a comprehensive list of references and sources.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
GHBP Human, HisDescription:
Growth Hormone Binding Protein Human Recombinant, His Tag
Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.
Product # :
CYT-921Price :
Quantity :
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Shipped with Ice Packs
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Description
GHBP produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 254 amino acids (19-264a.a.) and having a molecular mass of 29.4kDa.GHBP is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GHBP protein solution (1mg/ml) contains phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
The ED50 range ≤ 10ng/ml and is measured by ability to inhibit GH-induced proliferation assay using Nb2-11 Rat lymphoma cells in the presence of 1.25ng/ml of human growth hormone.
More Info
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Introduction
Growth hormone receptor, also known as GHR is part of the cytokine receptor family. GHR binds 2 receptor molecules and in this manner induces signal transduction through receptor dimerization. Furthermore, at high concentrations, growth hormone performs as an antagonist since there is a large difference in affinities at the respective binding sites. The antagonist action can be enhanced further by reducing binding in the low affinity binding site.
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Synonyms
Growth Hormone Receptor, Growth Hormone Binding Protein, Somatotropin Receptor GH Receptor, Serum Binding Protein, GHBP, GHIP.
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Physical Appearance
Sterile filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks.Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
FSGSEATAAI LSRAPWSLQS VNPGLKTNSS KEPKFTKCRS PERETFSCHW TDEVHHGTKN LGPIQLFYTR RNTQEWTQEW KECPDYVSAG ENSCYFNSSF TSIWIPYCIK LTSNGGTVDE KCFSVDEIVQ PDPPIALNWT LLNVSLTGIH ADIQVRWEAP RNADIQKGWM VLEYELQYKE
VNETKWKMMD PILTTSVPVY SLKVDKEYEV RVRSKQRNSG NYGEFSEVLY VTLPQMSQFT CEEDFYLEHH HHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
MIF Mouse, HisDescription:
Macrophage Migration Inhibitor Factor Mouse Recombinant, His Tag
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
Product # :
CYT-896Price :
Quantity :
Shipping Method :
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Description
MIF Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 138 amino acids (1-115 a.a) and having a molecular mass of 14.9kDa. MIF is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MIF protein solution (0.5mg/ml) containing Phosphate buffered saline , 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
The cytokine Macrophage migration inhibitory factor (MIF) has been identified to be secreted by the pituitary gland and the monocyte/macrophage and to play an important role in endotoxic shock. MIF has the unique property of being released from macrophages and T cells in response to physiological concentrations of glucocorticoids. The secretion of MIF is tightly regulated and decreases at high, anti-inflammatory steroid concentration.
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Synonyms
Macrophage migration inhibitory factor, MIF, Delayed early response protein 6, DER6, Glycosylation-inhibiting factor, GIF, L-dopachrome isomerase, L-dopachrome tautomerase, Phenylpyruvate tautomerase.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMPMFIVN TNVPRASVPE GFLSELTQQL AQATGKPAQY IAVHVVPDQL MTFSGTNDPC ALCSLHSIGK IGGAQNRNYS KLLCGLLSDR LHISPDRVYI NYYDMNAANV GWNGSTFA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
RELM g Mouse, HisDescription:
RELM-Gamma Mouse Recombinant, His Tag
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
Product # :
CYT-455Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
RELM-gamma Mouse Recombinant is a His -Tagged Fusion Protein having a molecular weight of 11 kDa containing 86 amino acid residues of the RELM-gamma Mouse and 16 additional amino acid residues – HisTag (underlined).
Source
Escherichia Coli.
Formulation
Filtered (0.4µm) and lyophilized from 0.5 mg/ml in 0.05M Acetate buffer pH-4.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
RELM-gamma is a novel member of the resistin-like molecule/found in inflammatory zone (RELM/FIZZ) family in mice and rats. Microarray and real-time RT-PCR experiments revealed a repression of RELMgamma mRNA in nasal respiratory epithelium of cigarette smoke-exposed versus untreated rats. The analysis of the physiological tissue-specific expression revealed highest expression in hematopoietic tissues, suggesting a cytokine-like role for RELM-gamma. RELM-gamma-mRNA is detectable in bone marrow, spleen, and lung as well as in peripheral blood granulocytes. Promyelocytic HL60 cells transfected with a RELM-gamma expression plasmid have an increased proliferation rate compared to mock-transfected cells and display an altered response to retinoic acid-induced granulocytic differentiation. Taken together, these data provide the first experimental evidence that RELM-gamma is a secreted molecule with a restricted expression pattern that may play a role in promyelocytic differentiation.
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Synonyms
Resistin-like gamma, RELMgamma,RELM-γ, RELM-g.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.The lyophilized protein remains stable until the expiry date when stored at -20°C.
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Solubility
It is recommended to add 0.1M Acetate buffer pH4 to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. For conversion into higher pH value, we recommend intensive dilution by relevant buffer to a concentration of 10µg/ml. In higher concentrations the solubility of this antigen is limited. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
MRGSHHHHHH GMASHMTLES IVEKKVKELL ANRDDCPSTV TKTFSCTSIT ASGRLASCPS GMTVTGCACG YGCGSWDIRD GNTCHCQCST MDWATARCCQ LA.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SIRPA Human, HEKDescription:
Signal-Regulatory Protein Alpha Human Recombinant, HEK
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptorSHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR.
Product # :
PRO-2755Price :
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Description
SIRPA Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-373a.a) containing 356 amino acids and having a molecular mass of 39kDa.SIRPA is fused to a 6 amino acid His-tag at C-terminus,and is purified by proprietary chromatographic techniques.
Source
HEK293 Cells.
Formulation
The SIRPA solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
Measured by its binding ability in a functional ELISA with Human CD47.
More Info
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Introduction
Signal-Regulatory Protein Alpha, SIRPA belongs to the signal-regulatory-protein (SIRP) family, as well as the immunoglobulin super family. The members of the SIRP family are receptor-type transmembrane glycoproteins which are involved in the negative regulation of receptor tyrosine kinase-coupled signaling processes.
SIRPA can be phosphorylated by tyrosine kinases. The phospho-tyrosine residues of this PTP have been shown to recruit SH2 domain containing tyrosine phosphatases (PTP), and perform as substrates of PTPs. SIRPA take part in signal transduction mediated by a variety of growth factor receptors. CD47 has been shown to be a ligand for SIRPA. -
Synonyms
Tyrosine-protein phosphatase non-receptor type substrate 1 isoform 1, SHP substrate 1, SHPS-1, Brain Iglike molecule with tyrosine-based activation motifs, Bit, CD172 antigen-like family member A, MYD1, PTPNS1, SHPS1,SIRP, Inhibitory receptor
SHPS-1, Macrophage fusion receptor, MyD-1 antigen, Signal-regulatory protein alpha-1, Sirp-alpha-1, Signalregulatory protein alpha-2, Sirp-alpha-2, Signal-regulatory protein alpha-3, Sirp-alpha-3, p84, CD172a, BIT, MFR. -
Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
DGSGVAGEEE LQVIQPDKSV LVAAGETATL RCTATSLIPV GPIQWFRGAG PGRELIYNQK EGHFPRVTTV SDLTKRNNMD FSIRIGNITP ADAGTYYCVK FRKGSPDDVE FKSGAGTELS VRAKPSAPVV SGPAARATPQ HTVSFTCESH GFSPRDITLK WFKNGNELSD FQTNVDPVGE SVSYSIHSTA KVVLTREDVH SQVICEVAHV TLQGDPLRGT ANLSETIRVP PTLEVTQQPV RAENQVNVTC QVRKFYPQRL QLTWLENGNV SRTETASTVT ENKDGTYNWM SWLLVNVSAH RDDVKLTCQV EHDGQPAVSK SHDLKVSAHP KEQGSNTAAE NTGSNERNIY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
PODXL HumanDescription:
Podocalyxin-Like Human Recombinant
Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.
Product # :
PRO-2768Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PODXL Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain containing 416 amino acids (23-429 a.a.) and having a molecular mass of 43.1 kDa. PODXL is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
HEK293 Cells
Formulation
PODXL protein solution (1mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.
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Synonyms
Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
DGS-SPSPSPS PSQNATQTTT DSSNKTAPTP ASSVTIMATD TAQQSTVPTS KANEILASVK ATTLGVSSDS PGTTTLAQQV SGPVNTTVAR GGGSGNPTTT IESPKSTKSA DTTTVATSTA TAKPNTTSSQ NGAEDTTNSG GKSSHSVTTD LTSTKAEHLT TPHPTSPLSP RQPTSTHPVA TPTSSGHDHL MKISSSSSTV AIPGYTFTSP GMTTTLPSSV ISQRTQQTSS QMPASSTAPS SQETVQPTSP ATALRTPTLP ETMSSSPTAA STTHRYPKTP SPTVAHESNW AKCEDLETQT QSEKQLVLNL TGNTLCAGGA SDEKLISLIC RAVKATFNPA QDKCGIRLAS VPGSQTVVVK EITIHTKLPA KDVYERLKDK WDELKEAGVS DMKLGDQGPP EEAEDRFSMP-HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
CANX AntibodyDescription:
Mouse Anti Human Calnexin
Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.
Product # :
ANT-713Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- More Info
Formulation
1mg/ml containing PBS, pH-7.4, 10% Glycerol and 0.02% Sodium Azide.
More Info
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Introduction
Calnexin (CANX) belongs to the calnexin family of molecular chaperones. Calnexin is a calcium-binding, ER-associated protein that interacts briefly with newly synthesized N-linked glycoproteins, facilitating protein folding and assembly. Calnexin may also have a key role in the quality control of protein folding by retaining incorrectly folded protein subunits within the ER for degradation. Calnexin grants long-term protection of wild-type Shaker protein from ER-associated degradation. Polypeptide substrate recognition by Calnexin requires specific conformations of the Calnexin protein. Calnexin dwindles with aging and might contribute to a cytoprotection in an array of human age-related diseases.
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Synonyms
Calnexin, Major histocompatibility complex class I antigen-binding protein p88, p90, IP90, CANX, CNX, FLJ26570.
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Physical Appearance
Sterile filtered colorless solution.
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Immunogen
Anti-human CANX mAb, is derived from hybridization of mouse F0 myeloma cells with spleen cells from BALB/c mice immunized with a recombinant human CANX protein 21-481 amino acids purified from E. coli.
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Ig Subclass
Mouse IgG1 heavy chain and k light chain.
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Clone
PAT18B9AT.
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Applications
CANX antibody has been tested by ELISA and Western blot analysis to assure specificity and reactivity. Since application varies, however, each investigation should be titrated by the reagent to obtain optimal results.
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Type
Mouse Anti Human Monoclonal.
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Storage Procedures
For periods up to 1 month store at 4°C, for longer periods of time, store at -20°C. Prevent freeze thaw cycles.
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Purification Method
CANX antibody was purified from mouse ascitic fluids by protein-A affinity chromatography.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
b NGF Human, HEKDescription:
beta Nerve Growth Factor Human Recombinant, HEK
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
Product # :
CYT-079Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
BNGF Human Recombinant produced in HEK293 is a noncovalently disulfide linked homodimer, glycosylated, polypeptide chain (Ser122-Arg239) containing 2 identical 118 amino acids and having a molecular mass of 26.5 kDa.
Source
HEK293 cells.
Formulation
The b-NGF was lyophilized from 1mg/ml in 20mM PB and 0.25M NaCl pH-7.5.
Purity
Greater than 97% as obsereved by SDS-PAGE.
Biological Activity
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.
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Introduction
NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.
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Synonyms
Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized b-NGF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution b-NGF should be stored at 4°C between 2-7 days and for future use below -18°C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized b-NGF in sterile distilled pyrogen free water at a concentration of 0.25mg/ml.
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Background
What is the molecular weight/Mw of B NGF Protein?
B NGF Protein has a total Mw of 26.5kDa.
What is the source or expression system of B NGF Protein?
HEK293 cells.
What is the Purity of B NGF Protein?
B NGF Protein is >97% pure as determined by SDS-PAGE.
What is the Biological Activity of B NGF Protein?
The specific activity was determined by the dose-dependent stimulation of the proliferation of human TF-1 cells (human erythroleukemic indicator cell line), the ED50 is <0.04-0.4ng/ml.
What is the amino acid sequence of B NGF Protein?
B NGF Protein is composed from 118 amino acids.
What applications can B NGF Protein be used in?
B NGF Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for B NGF Protein?
The endotoxin level is minimal, B NGF Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
SOST Human, HEKDescription:
Sclerostin Human Recombinant, HEK
Sclerostin, SOST, CDD, VBCH.
Product # :
PRO-2481Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
SOST Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 24-213) containing 196 amino acids including a 6 a.a C-terminal His tag. The total molecular mass is 22.4kDa (calculated).
Source
HEK293 Cells.
Formulation
SOST filtered (0.4 µm) and lyophilized from 0.5mg/ml in PBS and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Sclerostin (SOST) is a secreted glycoprotein with a C-terminal cysteine knot-like (CTCK) domain and sequence similarity to the DAN (differential screening-selected gene aberrative in neuroblastoma) family of bone morphogenetic protein (BMP) antagonists. Sclerostin functions as a negative regulator of bone growth, by inhibiting bone formation. SOST is widely expressed at low levels, with highest levels in the bone, cartilage, kidney, liver, bone marrow and primary osteoblasts differentiated for 21 days. SOST gene defects cause sclerosteosis and bone dysplasia.
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Synonyms
Sclerostin, SOST, CDD, VBCH.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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Stability
Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. SOST is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
QGWQAFKNDA TEIIPELGEY PEPPPELENN KTMNRAENGG RPPHHPFETK DVSEYSCREL HFTRYVTDGP CRSAKPVTEL VCSGQCGPAR LLPNAIGRGK WWRPSGPDFR CIPDRYRAQR VQLLCPGGEA PRARKVRLVA SCKCKRLTRF HNQSELKDFG TEAARPQKGR KPRPRARSAK ANQAELENAY HHHHHH.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TAF10 HumanDescription:
TAF10 RNA Polymerase II Human Recombinant
TAF10 RNA Polymerase II TATA Box Binding Protein (TBP)-Associated Factor 30kDa, Transcription Initiation Factor TFIID 30 KDa Subunit, STAF28, TAF2A, TAF2H.
Product # :
ENZ-750Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TAF10 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (84-218) and having a molecular mass of 16.9kDa.TAF10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TAF10 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TAF10 is a small subunit of TFIID which is related to a subdivision of TFIID complexes. Studies with human and mammalian cells verified that this subunit is mandatory for transcriptional activation by the estrogen receptor, for progression through the cell cycle, and is essential for several cellular differentiation programs.
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Synonyms
TAF10 RNA Polymerase II TATA Box Binding Protein (TBP)-Associated Factor 30kDa, Transcription Initiation Factor TFIID 30 KDa Subunit, STAF28, TAF2A, TAF2H.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSGAAPPEG AISNGVYVLP SAANGDVKPV VSSTPLVDFL MQLEDYTPTI PDAVTGYYLN RAGFEASDPR IIRLISLAAQ KFISDIANDA LQHCKMKGTA SGSSRSKSKD RKYTLTMEDL TPALSEYGIN VKKPHYFT
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TGFB1 Human, HisDescription:
Transforming Growth Factor-Beta 1 Human Recombinant, His Tag
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
Product # :
CYT-672Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
TGF-b 1 Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing 112 amino acids fragment (279-390) having a molecular weight of 17.3kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The TGF-b 1 His is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
TGF-b 1 His-Tag protein is supplied in 25mM NaAcetate pH 4.8 and 50% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.
TGF-b 1 regulates the actions of numerous other growth factors involved in a variety of human diseases including renal disease, hepatic disease, heart failure and cardiomyopathies. -
Synonyms
Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1, TGFB1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
PODXL MouseDescription:
Podocalyxin-Like Mouse Recombinant
Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.
Product # :
PRO-2310Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
PODXL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (22-404a.a.) and having a molecular mass of 41.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). PODXL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PODXL protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.
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Synonyms
Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.
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Physical Appearance
Sterile Filtered clear solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.
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Amino Acid Sequence
HNGNETSTSA IKSSTVQSHQ SATTSTEVTT GHPVASTLAS TQPSNPTPFT TSTQSPSMPT STPNPTSNQS GGNLTSSVSE VDKTKTSSPS STAFTSSSGQ TASSGGKSGD SFTTAPTTTL GLINVSSQPT DLNTTSKLLS TPTTDNTTSP QQPVDSSPST ASHPVGQHTP AAVPSSSGST PSTDNSTLTW KPTTHKPLGT SEATQPLTSQ TPGITTLPVS TLQQSMASTV GTTTEEFTHL ISNGTPVAPP GPSTPSPIWA FGNYQLNCEP PIRPDEELLI LNLTRASLCE RSPLDEKEKL VELLCHSVKA SFKPAEDLCT LHVAPILDNQ AVAVKRIIIE TKLSPKAVYE LLKDRWDDLT EAGVSDMKLG KEGPPEVNED RFSLEHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Name :
TXN1, HisDescription:
Thioredoxin Recombinant, His Tag
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
Product # :
PRO-784Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
Recombinant Thioredoxin produced in E.Coli is a single, non-glycosylated polypeptide chain containing 117 amino acids (2-109 a.a.) and having a molecular mass of 12.8kDa. TRX contains 9 amino acid His Tag N-terminus and is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TRX His Tag protein solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Biological Activity
Specific activity is >70 A650/cm/min/mg, detected by measuring the increase of insulin precipitation in absorbance at 650 nm resulting from the reduction of insulin.
More Info
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Introduction
Thioredoxins are small disulphide-containing redox proteins (within the conserved Cys-Gly-Pro-Cys active site) that have been found in all the kingdoms of living organisms. Thioredoxin contains a single disulfide active site and serves as a general protein disulphide oxidoreductase. Thioredoxins are involved in the first unique step in DNA synthesis. It interacts with a broad range of proteins by a redox mechanism based on reversible oxidation of two cysteine thiol groups to a disulphide, accompanied by the transfer of two electrons and two protons. The net result is the covalent interconversion of a disulphide and a dithiol. Trx also provides control over a number of transcription factors affecting cell proliferation and death through a mechanism referred to as redox regulation. It has been suggested that thioredoxin may catalyze the formation of correct disulfides during protein folding because of its ability to act as an efficient oxidoreductant. This could be especially useful in
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Synonyms
Thioredoxin-1, Trx-1, trxA, fipA, tsnC, b3781, JW5856.
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Physical Appearance
Sterile Filtered colorless solution.
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Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
MHHHHHHMGS DKIIHLTDDS FDTDVLKADG AILVDFWAEW CGPCKMIAPI LDEIADEYQG KLTVAKLNID QNPGTAPKYG IRGIPTLLLF KNGEVAATKV GALSKGQLKE FLDANLAGS.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.