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Search results

1000 results found for “Stathmin”

Name

Description

Product #

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  • View Data Sheet

    Name :

    SNAI1 Human

    Description:

    Snail Family Zinc Finger 1 Human Recombinant

    Snail Family Zinc Finger 1, Protein Sna, Protein Snail Homolog 1, SNAH, Snail 1 (Drosophila Homolog), Zinc Finger Protein, Snail Homolog 1 (Drosophila), SLUGH2, SNA, SNAIL, SNAIL1, dJ710H13.1, Snail 1 Homolog, Snail 1 Zinc Finger Protein, Snail 1, Zinc Finger Protein, Snail Homolog 1, Zinc Finger Protein SNAI1.

    Product # :

    PRO-1759

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    Description

    SNAI1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 287 amino acids (1-264 a.a) and having a molecular mass of 31.5kDa.SNAI1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNAI1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.4M urea and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Snail homolog 1 (SNAI1) is involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. SNAI1 binds to 3 E-boxes of the E-cadherin gene promoter and represses its transcription. The nuclear protein encoded by SNAI1 is structurally identical to the Drosophila snail protein, and is considered as well to be vital for mesoderm formation in the developing embryo. At least two variants of a similar processed pseudogene have been found on chromosome 2. Among the diseases associated with SNAI1 are waardenburg syndrome type iid, and inappropriate adh syndrome.

    • Synonyms

      SnailFamily ZincFinger 1, Protein Sna, Protein Snail Homolog 1, SNAH, Snail 1 (Drosophila Homolog), Zinc Finger Protein, Snail Homolog 1 (Drosophila), SLUGH2, SNA, SNAIL, SNAIL1, dJ710H13.1, Snail 1 Homolog, Snail 1 Zinc Finger Protein, Snail 1, Zinc Finger Protein, Snail Homolog 1, Zinc Finger Protein SNAI1.

    • Physical Appearance

      Sterile Filtered clear 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).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMPRSFLV RKPSDPNRKP NYSELQDSNP EFTFQQPYDQ AHLLAAIPPP EILNPTASLP MLIWDSVLAP QAQPIAWASL RLQESPRVAE LTSLSDEDSG KGSQPPSPPS PAPSSFSSTS VSSLEAEAYA AFPGLGQVPK QLAQLSEAKD LQARKAFNCK YCNKEYLSLG ALKMHIRSHT LPCVCGTCGK AFSRPWLLQG HVRTHTGEKP FSCPHCSRAF ADRSNLRAHL QTHSDVKKYQ CQACARTFSR MSLLHKHQES GCSGCPR

    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.

    Snai1 Human
  • View Data Sheet

    Name :

    SRI Human

    Description:

    Sorcin Human Recombinant

    Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

    Product # :

    PRO-166

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    Description

    SRI Human Recombinant fused with a 23 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 221 amino acids (1-198 a.a.) and having a molecular mass of 24.1kDa. The SRI is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SRI solution (0.5 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.2M NaCl, 1mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Sorcin (SRI) which is a 22kDa calcium-binding protein was originally identified in multidrug-resistant cells. Sorcin, which modulates excitation-contraction coupling in the heart, contributes to calcium homeostasis in the heart sarcoplasmic reticulum.

    • Synonyms

      Sorcin, 22 kDa protein, CP-22, CP22, V19, SRI, SCN, FLJ26259.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMAYPGHP GAGGGYYPGG YGGAPGGPAF PGQTQDPLYG YFAAVAGQDG QIDADELQRC LTQSGIAGGY KPFNLETCRL MVSMLDRDMS GTMGFNEFKE LWAVLNGWRQ HFISFDTDRS GTVDPQELQK ALTTMGFRLS PQAVNSIAKR YSTNGKITFD DYIACCVKLR ALTDSFRRRD TAQQGVVNFP YDDFIQCVMS V.

    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.

    Sri Human
  • View Data Sheet

    Name :

    OSM Human, His

    Description:

    Oncostatin-M Human Recombinant, His Tag

    OSM, MGC20461.

    Product # :

    CYT-060

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    • description
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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

    • 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.

    • Synonyms

      OSM, MGC20461.

    • 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.

    • 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.

    Osm Human His
  • View Data Sheet

    Name :

    PALM Human

    Description:

    Paralemmin Human Recombinant

    Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.

    Product # :

    PRO-2053

    Price :

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    • description
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    Description

    PALM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (1-387) and having a molecular mass of 44.5kDa.PALM is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The PALM solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Paralemmin (PALM) belongs to the paralemmin protein family which takes part in plasma membrane dynamics and cell process formation. The product of PALM is related with the cytoplasmic face of plasma membranes and is implicated in plasma membrane dynamics in neurons and other cell types.

    • Synonyms

      Paralemmin-1, Paralemmin, PALM, KIAA0270, Paralemmin-1 isoform 1.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMEVLAAE TTSQQERLQA IAEKRKRQAE IENKRRQLED ERRQLQHLKS KALRERWLLE GTPSSASEGD EDLRRQMQDD EQKTRLLEDS VSRLEKEIEV LERGDSAPAT AKENAAAPSP VRAPAPSPAK EERKTEVVMN SQQTPVGTPK DKRVSNTPLR TVDGSPMMKA AMYSVEITVE KDKVTGETRV LSSTTLLPRQ PLPLGIKVYE DETKVVHAVD GTAENGIHPL SSSEVDELIH KADEVTLSEA GSTAGAAETR GAVEGAARTT PSRREITGVQ AQPGEATSGP PGIQPGQEPP VTMIFMGYQN VEDEAETKKV LGLQDTITAE LVVIEDAAEP KEPAPPNGSA AEPPTEAASR EENQAGPEAT TSDPQDLDMK KHRCKCCSIM.

    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.

    Palm Human
  • View Data Sheet

    Name :

    TIMP2 Human, His

    Description:

    Tissue Inhibitor of Metalloprotease 2 Human Recombinant, His Tag

    TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.

    Product # :

    ENZ-646

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    • description
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    • More Info

    Description

    TIMP2 Human Recombinant produced in E. coli is a single polypeptide chain containing 232 amino acids (27-220) and having a molecular mass of 26.1 kDa.TIMP2 is fused to a 38 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TIMP2 solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      TIMP2 belongs to the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases that take part in degradation of the extracellular matrix. Besides having an inhibitory role against metalloproteinases, the encoded protein has a exclusive part among TIMP family members in its capability to directly suppress the proliferation of endothelial cells. Consequently, the encoded protein is crucial to the conservation of tissue homeostasis by suppressing the production of quiescent tissues as an answer to angiogenic factors, and by inhibiting protease activity in tissues undergoing renovation of the extracellular matrix.

    • Synonyms

      TIMP metallopeptidase inhibitor 2, metalloproteinase inhibitor 2, Tissue inhibitor of metalloproteinases 2, TIMP-2, CSC-21K.

    • 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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHM CS CSPVHPQQAF CNADVVIRAK AVSEKEVDSG NDIYGNPIKR IQYEIKQIKM FKGPEKDIEF IYTAPSSAVC GVSLDVGGKK EYLIAGKAEG DGKMHITLCD FIVPWDTLST TQKKSLNHRY QMGCECKITR CPMIPCYISS PDECLWMDWV TEKNINGHQA KFFACIKRSD GSCAWYRGAA PPKQEFLDIE DP

    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.

    Timp2 Human
  • View Data Sheet

    Name :

    GMNN Human

    Description:

    Geminin Human Recombinant

    GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    Product # :

    PRO-579

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    Description

    Geminin Human Recombinant fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids and having a molecular mass of 27.7 kDa.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris pH 8, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Geminin is a 25 kDa nuclear protein, which inhibits DNA replication and is degraded during the mitotic phase of the cell cycle. Geminin controls replication by binding to the licensing factor Cdt1, and is involved in neural differentiation. In addition, Geminin directly interacts with Six3 and Hox homeodomain proteins during embryogenesis and inhibits their functions. Geminin can also promote DNA replication. Geminin has 2 roles in 2 different stages of the cell cycle: Geminin is a negative regulator of DNA replication during the “S phase” of the cell cycle. Inhibition of Geminin during the “S phase” (by RNAi) results in an additional round of replication of portions of the genome. During the “M phase” of the cell cycle (mitosis) Geminin stabilizes the replication factor Cdt1 promoting DNA replication during the next cell cycle. Moreover, inhibition of Geminin during mitosis (by RNAi) causes destabilization of Cdt1 protein and impairment of DNA replication during the next cell cycle. Geminin thus guarantees that only one round of replication occurs during each cell cycle. It was discovered that Geminin is overexpressed in a number of malignancies and cancer cell lines. This maintains the concept that Geminin has also a positive role in DNA replication and cell cycle progression. Geminin accumulates through S, G2 and M phases of the cell cycle but is absent during the G1 phase. During the metaphase/anaphase transition of mitosis Geminin levels decrease.

    • Synonyms

      GMNN, Geminin, DNA Replication Inhibitor, Gem, RP3-369A17.3.

    • 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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMNPS MKQKQEEIKE NIKNSSVPRR TLKMIQPSAS GSLVGRENEL SAGLSKRKHR NDHLTSTTSS PGVIVPESSE NKNLGGVTQE SFDLMIKENP SSQYWKEVAE KRRKALYEAL KENEKLHKEI EQKDNEIARL KKENKELAEV AEHVQYMAEL IERLNGEPLD NFESLDNQEF DSEEETVEDS LVEDSEIGTC AEGTVSSSTD
      AKPCI.

    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.

    Geminin Human
  • View Data Sheet

    Name :

    GST S. Japonicum, His

    Description:

    Glutathione S-Transferase Schistosoma Japonicum Recombinant, His

    Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase. 

    Product # :

    ENZ-1146

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    Description

    GST S. Japonicum Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 244 amino acids (1-218) and having a molecular mass of 28.3 kDa.GST S. Japonicum is fused to a 26 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GST S. Japonicum protein solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 10unit/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    More Info

    • Introduction

      Glutathione S-transferase or GST, stands for a large family of detoxification proteins and enzymes. Glutathione S-transferase catalyzes glutathione reaction and an acceptor molecule to create S-substituted glutathione (S stands for sulfur). By this reaction, a large variety of compounds, for example therapeutic drugs, carcinogens & oxidative stress products, transformed. Glutathione S-transferase acts as a transport protein by binding toxins and acts as a transport protein. At first, the protein was isolated from Schistosomajaponicum, nowadays it is isolated from E. coli bacteria.

    • Synonyms

      Glutathione S-Transferase class-mu 26 kDa isozyme, Sj26 antigen, SjGST, Glutathione S-Transferase class-mu 26 kDa isozyme Glutathione S Transferase.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPKSD
      LVPR

    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.

    Gst S Japonicum
  • View Data Sheet

    Name :

    GZMH Human, sf9

    Description:

    Granzyme-H Human Recombinant, sf9

    Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.

    Product # :

    ENZ-961

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    Description

    GZMH produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (19-246 a.a.) and having a molecular mass of 26.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    GZMH protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.

    • Synonyms

      Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.

    • 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.

    • Amino Acid Sequence

      EEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPPGV YIKVSHFLPW IKRTMKRLHH 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.

    Gzmh Human Sf9
  • View Data Sheet

    Name :

    Gly m 4.0101

    Description:

    Stress-Induced Protein SAM22 Recombinant

    Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    Product # :

    PRO-2278

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    Description

    Recombinant Stress-Induced Protein SAM22 produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 19,484 Dalton. Gly m 4.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    Gly m 4.0101 is supplied in in 20mM HEPES buffer pH-7.9 and 6M Urea.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

    • Synonyms

      Stress-induced protein SAM22, Starvation-associated message 22, Gly m 4.

    • Physical Appearance

      Sterile Filtered clear 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgE type human antibodies. 2. Immunodot test with positive/negative sera panels.

    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.

    Gly M 40101
  • View Data Sheet

    Name :

    CSTA Human, His

    Description:

    Cystatin A Human Recombinant, His tag

    Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    Product # :

    PRO-504

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    Description

    CSTA produced in E.Coli is a single, non-glycosylated polypeptide chain containing 118 amino acids (1-98 a.a.) and having a molecular mass of 13.1kDa.CSTA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Cystatin-A (1mg/ml) in 20mM Tris-HCl buffer (pH8.0), 1mM DTT and 10% glycerol.

    More Info

    • Introduction

      Cystatin-A is the intracellular inhibitor of cysteine proteinase cathepsin B (CatB) and belongs to family 1 of the cystatin superfamily of inhibitor proteins. CSTA is a stefin that functions as a cysteine protease inhibitor, forming tight complexes with papain and the cathepsins B, H, and L. It has been proposed that extracellular CatB together with other classes of proteinases are all subjected to a cascade-like manner of activation. CatB and its inhibitor Cystatin-A are involved in degradation of extracellular matrix proteins during tissue remodeling. CSTA is one of the precursor proteins of cornified cell envelope in keratinocytes and plays a role in epidermal development and maintenance. Cystatin-A has been reported to be found in high concentrations in epithelial cells, polymorphonuclear leukocytes and lymphoid tissue. Stefins may be used as prognostic and diagnostic tools for cancer.

    • Synonyms

      Cystatin-A, Cystatin-AS, Stefin-A, CSTA, STF1, STFA.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MIPGGLSEAK PATPEIQEIV DKVKPQLEEK TNETYGKLEA VQYKTQVVAG TNYYIKVRAG DNKYMHLKVF KSLPGQNEDL VLTGYQVDKN KDDELTGF.

    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.

    Csta Human His
  • View Data Sheet

    Name :

    SCF Canine

    Description:

    Stem Cell Factor Canine Recombinant

    Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.

    Product # :

    CYT-194

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    Description

    Stem Cell Factor Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18.4kDa Dalton. The SCF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.

    Purity

    Greater than 97.0% as determined by HPLC and SDS-PAGE.

    Biological Activity

    Fully biologically active when compared to standard. The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF-1 cells is less than 2.0ng/ml, corresponding to a specific activity of 5,000,000IU/mg.

    More Info

    • Introduction

      Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).

    • Synonyms

      Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      KGICGKRVTD DVKDVTKLVA NLPKDYKIAL KYVPGMDVLP SHCWISVMVE QLSVSLTDLL DKFSNISEGL SNYSIIDKLV KIVDDLVECT EGYSFENVKK APKSPELRLF TPEEFFRIFN RSIDAFKDLE TVASKSSECV VSSTLSPDKD SRVSVTKPFM LPPVA

    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.

    Scf K9
  • View Data Sheet

    Name :

    SUGT1 Human

    Description:

    SGT1 Recombinant Human

    SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae), SGT1, Putative 40-6-3 protein, SGT1B protein.

    Product # :

    PRO-096

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    Description

    SGT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (115-365.a.a) and having a molecular mass of 30.7kDa. SGT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SGT1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SUGT1 is homolog to yeast protein SGT1, a regulator of the cell cycle which is vital for G1/S and G2/M transitions. SUGT1 holds a CS domain, a SGS domain, a p23 domain and three tetratricopeptide repeats (TPR). SUGT1 protein associates with Skp1 p19 and CUL-1, subunits of the SCF ubiquitin ligase complex, and is believed to take a part in protein degradation. Furthermore, SUGT1 is essential for the kinetochores assembly, and has a role as a co-chaperone for HSP90.

    • Synonyms

      SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae), SGT1, Putative 40-6-3 protein, SGT1B protein.

    • Physical Appearance

      Sterile Filtered clear 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.Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MHRVGQAGLQ LLTSSDPPAL DSQSAGITGA DANFSVWIKR CQEAQNGSES EVWTHQSKIK YDWYQTESQVVITLMIKNVQ KNDVNVEFSE KELSALVKLP SGEDYNLKLE LLHPIIPEQS TFKVLSTKIE IKLKKPEAVR WEKLEGQGDV PTPKQFVADVKNLYPSSSPY TRNWDKLVGE IKEEEKNEKL EGDAALNRLF QQIYSDGSDE VKRAMNKSFM ESGGTVLSTN WSDVGKRKVE INPPDDMEWKKY

    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.

    Sugt1 Human
  • View Data Sheet

    Name :

    RNP/Sm Bovine

    Description:

    Bovine RNP/Sm Ribonucleoprotein Complex

    Product # :

    PRO-2556

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    Description

    RNP/Sm Bovine is purified from bovine tissues by proprietary protein-chemical techniques.

    Source

    Bovine tissues.

    Formulation

    RNP/Sm Bovine is supplied in 20mM HEPES buffer pH-8, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      U-snRNPs which are a pivotal part of spliceosomes, are created between small non-coding nuclear RNAs and a protein moiety. Whereas the 7 Sm proteins are conserved, the RNP antigens are exclusive for each U-snRNP subclass.

    • Physical Appearance

      Sterile Filtered clear 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. Avoid multiple freeze-thaw cycles.

    • Immunological Functions

      1. Binds IgG type human auto antibodies.2. Immunodot test with positive/negative samples.

    • Applications

      Western blot with anti-RNP/Sm autoantibody positive sample.

    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.

    Rnpsm
  • View Data Sheet

    Name :

    IFNG Mouse

    Description:

    IFN-Gamma Mouse Recombinant

    Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    Product # :

    CYT-358

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    Description

    IFN-gamma Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 134 amino acids and having a molecular mass of 15.6kDa.The IFN-gamma is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution in PBS, pH 7.4 and 5% trehalose.

    Purity

    Greater than 95.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg

     

    More Info

    • Introduction

      IFN-gamma produced by lymphocytes activated by specific antigens or mitogens.
      IFN-gamma, in addition to having antiviral activity, has important immunoregulatory functions, it is a potent activator of macrophages, and has antiproliferative effects on transformed cells and it can potentiate the antiviral and antitumor effects of the type I IFNs.

    • Synonyms

      Immune IFN, type II IFN, T cell IFN, MAF, IFNG, IFG, IFI, IFN-gamma.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized IFN-gamma although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IFN-gamma 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.

    • Solubility

      It is recommended to reconstitute the lyophilized IFN-gamma in sterile distilled water or 20mM AcOH at concentrations ranging between 0.1mg-0.5mg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

    • Background

      What is the molecular weight/Mw of IFNG MOUSE Protein?
      IFNG MOUSE Protein has a total Mw of 15.6kDa.

      What is the source or expression system of IFNG MOUSE Protein?
      Escherichia Coli.

      What is the Purity of IFNG MOUSE Protein?
      IFNG MOUSE Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of IFNG MOUSE Protein?
      The specific activity as determined in a viral resistance assay is < 0.1 ng/ml, corresponding to a specific activity of 10,000,000 IU/mg


      What is the amino acid sequence of IFNG MOUSE Protein?
      MHGTVIESLE SLNNYFNSSG IDVEEKSLFL DIWRNWQKDG DMKILQSQII SFYLRLFEVL KDNQAISNNI SVIESHLITT FFSNSKAKKD AFMSIAKFEV NNPQVQRQAF NELIRVVHQL LPESSLRKRK RSRC.

      What applications can IFNG MOUSE Protein be used in?
      IFNG MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for IFNG MOUSE Protein?
      The endotoxin level is minimal, IFNG MOUSE 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.

    Interferon Gamma Mouse
  • View Data Sheet

    Name :

    TSH Canine

    Description:

    Thyroid Stimulating Hormone Canine Recombinant

    Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

    Product # :

    HOR-049

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    Description

    TSH Canine is a heterodimeric glycoprotein consisting of 2 non-covalently linked subunits, an alpha subunit (96 a.a) and a beta subunit (118 a.a). TSH Canine is produced by co-expression of the alpha and beta subunits of TSH. Beta subunit contains alanine instead of valine at position 81.

    Source

    Mammalian cell line.

    Formulation

    TSH was lyophilized from 150mM NaCl, 10mM K-phosphate, pH 7.4, 0.1% CHAPS and 100mM D-mannitol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroid Stimulating Hormone 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.

    • Solubility

      It is recommended to reconstitute the lyophilized TSH in deionized H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Thyroid Stimulating Hormone (TSH), a pivotal glycoprotein hormone secreted by the anterior pituitary gland, stands as the master regulator of thyroid function. Its intricate control over thyroid hormone synthesis and secretion makes it a linchpin in the delicate balance of the endocrine system. The study of TSH, particularly in the form of TSH Recombinant Protein, has not only provided profound insights into thyroid physiology but has also revolutionized diagnostic methods, therapeutic interventions, and our understanding of various thyroid disorders. This research delves into the multifaceted realm of TSH, exploring its structural intricacies, physiological roles, and its far-reaching implications in both clinical and research settings.

      Structural Insights into TSH:

      TSH, a heterodimeric protein consisting of alpha and beta subunits, possesses a distinctive structure crucial for its biological activity. The beta subunit contains a unique hinge region, allowing flexibility in its interactions with the thyroid follicular cells. Understanding these structural nuances is fundamental for comprehending TSH's receptor binding, signaling cascades, and its intricate feedback mechanisms governing thyroid hormone production.

      Physiological Significance in Thyroid Regulation:

      TSH orchestrates thyroid function by binding to its specific receptors on the thyroid gland, stimulating iodine uptake, thyroid hormone synthesis, and secretion. This process is indispensable for maintaining the body's metabolism, energy balance, and overall growth and development. TSH's meticulous control over thyroid activity ensures the precise release of thyroid hormones, essential for numerous physiological processes and maintaining homeostasis.

      Diagnostic and Therapeutic Applications:

      In the realm of diagnostics, TSH assays utilizing TSH Recombinant Protein have revolutionized the detection and monitoring of thyroid disorders, particularly hypothyroidism and hyperthyroidism. By measuring TSH levels, clinicians can assess thyroid function, enabling early diagnosis and personalized treatment strategies. Moreover, recombinant TSH finds applications in diagnostic imaging, enhancing the accuracy of radioiodine scans for thyroid cancer diagnosis and treatment.

      Innovative Therapies and Future Prospects:

      Recombinant TSH has paved the way for innovative therapeutic interventions, particularly in the management of thyroid cancer. Thyroid remnant ablation, a crucial step in thyroid cancer treatment, involves the administration of radioiodine following recombinant TSH stimulation, maximizing the therapeutic efficacy while minimizing the radiation exposure to surrounding tissues. Ongoing research explores the potential of TSH receptor agonists and antagonists, offering new avenues for targeted therapies in thyroid-related disorders.

      TSH Recombinant Protein, with its profound influence on thyroid function and its applications in diagnostics and therapeutics, stands at the forefront of endocrine research. Its intricate roles in thyroid regulation, metabolism, and growth highlight its significance in human physiology. As our understanding of TSH deepens, it not only aids in the development of innovative treatments but also opens new avenues for exploring the complex interplay between hormones, receptors, and physiological responses. This research not only illuminates the vital role of TSH but also underscores its potential in shaping the future of thyroid-related healthcare.

      What is the source or expression system of TSH CANINE Protein?
      Mammalian cell line.

      What is the Purity of TSH CANINE Protein?
      TSH CANINE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of TSH CANINE Protein?
      The biological functionality of TSH CANINE Protein will be determined in the future.


      What applications can TSH CANINE Protein be used in?
      TSH CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for TSH CANINE Protein?
      The endotoxin level is minimal, TSH CANINE 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.

    Tsh Canine
  • View Data Sheet

    Name :

    SCGN Rat

    Description:

    Secretagogin Rat Recombinant

    SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

    Product # :

    PRO-657

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    Description

    Secretagogin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 286 amino acids and having a molecular mass of 33.3 kDa. The Rat SCGN is fused to a 10 a.a. His tag at N-Terminus.The protein’s amino acids sequence is identical to UniProtKB/Swiss-Prot entry Q6R556.The Rat SCGN is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The sterile filtered concentrated protein solution was lyophilized with 20mM Tris & 50mM NaCl pH-7.5.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SCGN is a secreted calcium-binding protein which is found in the cytoplasm. It is related to calbindin D-28K and calretinin. Secretagogin is involved in KCL-stimulated calcium flux and cell proliferation.
      Secretagogin plays a role in human non-functional pituitary adenomas.

    • Synonyms

      SCGN, EF-hand calcium binding protein, Setagin, SEGN, CALBL, Secretagogin.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • 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.

    • Solubility

      Add deionized water to a working concentration of 0.5mg/ml and let the lyophilized pellet dissolve completely.

    • Amino Acid Sequence

      MKHHHHHHAS MDNAHRQTQA HLDAACFWQI WQRFDKDEKG YIKETELDAF FDDLLAKFGI EDTLMEENVQ KMKEQLMVGH DISKEGRILM KELASMFLSE DENFLLFFRL ETPLDNSVEF MQIWRKYDAD SSGFISAAEL SNFLRDLFLH HKKVISEAEL EEYTSTMMKI FDRNKDGRLD LNDLARILAL QENFLLQFKM DASSTEERKR DFEKIFAHYD VSKTGALEGP EVDGFVKDMM ELVQPSISGV DLDKFREILL RHCDVNKDGK IQKSELALCLGLKINP.

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    Scgn Rat
  • View Data Sheet

    Name :

    SHFM1 Human

    Description:

    Split Hand/Foot Malformation Type 1 Human Recombinant

    SHFM1, Split Hand/Foot Malformation (Ectrodactyly) Type 1, DSS1, SHFD1, Deleted In Split Hand/Split Foot Protein 1, Split Hand/Foot Deleted Protein 1, Split Hand/Foot Malformation Type 1 Protein, Deleted In Split-Hand/Foot 1, 26S Proteasome Complex Subunit DSS1, ECD, SEM1, SHSF1, Shfdg1, Deleted In Split-Hand/Split-Foot 1, SHFDG1.

    Product # :

    PRO-1777

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    Description

    SHFM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 93 amino acids (1-70 a.a) and having a molecular mass of 10.7kDa (Molecular size on SDS-PAGE will appear higher).SHFM1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SHFM1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      26S proteasome complex subunit DSS1 (SHFM1) has been suggested as a candidate gene for the autosomal dominant form of the heterogeneous limb developmental disorder split hand/split foot malformation type 1. SHFM1 is a subunit of the 26S proteasome which plays a part in ubiquitin-dependent proteolysis. SHFM1 binds and stabilizes BRCA2 and is therefore involved in the control of R-loop-associated DNA damage and thus transcription-associated genomic instability. Furthermore, SHFM1 may have a role in the completion of the cell cycle. SHFM1 is a component of the TREX-2 complex (transcription and export complex 2), comprised of at least ENY2, GANP, PCID2, DSS1, and either centrin CETN2 or CETN3.

    • Synonyms

      SHFM1, Split Hand/Foot Malformation (Ectrodactyly) Type 1, DSS1, SHFD1, Deleted In Split Hand/Split Foot Protein 1, Split Hand/Foot Deleted Protein 1, Split Hand/Foot Malformation Type 1 Protein, Deleted In Split-Hand/Foot 1, 26S Proteasome Complex Subunit DSS1, ECD, SEM1, SHSF1, Shfdg1, Deleted In Split-Hand/Split-Foot 1, SHFDG1.

    • 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.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSEKKQP VDLGLLEEDD EFEEFPAEDW AGLDEDEDAH VWEDNWDDDN VEDDFSNQLR AELEKHGYKM ETS.

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    Shfm1 Human
  • View Data Sheet

    Name :

    Cardiac Actin Bovine

    Description:

    Cardiac Actin Bovine

    Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    Product # :

    PRO-519

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    Description

    Ultra pure Cardiac Actin having a Molecular mass of 43,000 dalton.

    Source

    Bovine Heart.

    Formulation

    The protein was lyophilized from a 1mg/ml solution containing 10mM Tris-acetate buffer pH 8.0, 0.2mM CaCl2, 0.2mM ATP, 1mM DTT and 0.5% SDS.

    Purity

    Greater than 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    More Info

    • Introduction

      Alpha-cardiac actin belongs to the actin family which is comprised of three main groups of actin isoforms, alpha, beta, and gamma. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. Defects in the cardiac actin have been associated with idiopathic dilated cardiomyopathy (IDC) and familial hypertrophic cardiomyopathy (FHC).

    • Synonyms

      Actin alpha cardiac muscle 1, Alpha-cardiac actin, ACTC1, ACTC.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Cardiac-Actin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cardiac Actin 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Cardiac Actin in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Applications

      Protein standard in 1D and 2D SDS gelelectrophoresis
      Immunoassays
      Immunization.

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    Cardiac Actin
  • View Data Sheet

    Name :

    GSTM1 Human, Sf9

    Description:

    Glutathione S-Transferase M1 Human Recombinant, Sf9

    GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    Product # :

    ENZ-1092

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    Description

    GSTM1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (1-218a.a.) fused to a 9 aa His Tag at C-terminus containing 227 amino acids and having a molecular mass of 26.8kDa. GSTM1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Insect cells.

    Formulation

    GSTM1 protein solution (0.5mg/ml) contains 40% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytosolic and membrane-bound types of GST are encoded by 2 different supergene families. There are 8 classes of the soluble cytoplasmic mammalian GST: alpha, kappa, mu, omega, pi, sigma, theta and zeta. The mu class of enzymes functions in the detoxification of electrophilic compounds, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress, by conjugation with glutathione. The genes encoding the mu class of enzymes are arranged in a gene cluster on chromosome 1p13.3 and aare highly polymorphic. These genetic differences can change an individual's resistance to carcinogens and toxins as well as affect the toxicity and efficacy of certain drugs. Null mutations of this class mu gene have been linked with the rise in a number of cancers.

    • Synonyms

      GST1, GTH4, GTM1, GSTM1-1, MGC26563, GSTM1a-1a, GSTM1b-1b, GSTM1, Glutathione S-transferase Mu 1, GST class-mu 1, Glutathione S-transferase GT8.7, pmGT10, GST 1-1.

    • 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.

    • Amino Acid Sequence

      ADPMPMILGY WDIRGLAHAI RLLLEYTDSS YEEKKYTMGD APDYDRSQWL NEKFKLGLDF PNLPYLIDGA HKITQSNAIL CYIARKHNLC GETEEEKIRV DILENQTMDN HMQLGMICYN PEFEKLKPKY LEELPEKLKL YSEFLGKRPW FAGNKITFVD FLVYDVLDLH RIFEPKCLDA FPNLKDFISR FEGLEKISAY MKSSRFLPRP VFSKMAVWGN KHHHHHH.

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    Gstm1 Protein
  • View Data Sheet

    Name :

    Angiostatin K1-4

    Description:

    Angiostatin Kringles 1-4 Human

    Product # :

    PRO-604

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    Description

    Human Angiostatin kringles 1-4 is produced from Human Fluid is a glycosylated polypeptide chain which migrates as a doublet 50 kDa on SDS-PAGE. The Ang K1-4 is purified by proprietary chromatographic techniques.

    Source

    Human Fluid.

    Formulation

    Lyophilized from a (1mg/ml) solution in containing 20mM Hepes buffer pH-8.2 & 20mM NaCl.

    Purity

    Greater than 98.0% as determined by SDS-PAGE.

    Biological Activity

    Human Angiostatin Kringles 1-4 significantly inhibits basic-FGF induced endothelial cell proliferation and migration at concentration ranging from 300nM-1.0 uM.

    More Info

    • Introduction

      There are several proteolytic fragments or specific domains of proteins that act as inhibitors of angiogenesis. These include fragments of plasminogen such as Angiostatin protein kringles 1-4 and kringles 1-5, Endostatin, Restin, PEX, the N-terminal fragment of prolactin, and the Nterminally truncated platelet factor. Angiostatin is a proteolytic protein fragment of plasminogen that is comprised of the first 4 kringle regions. Angiostatin k1-4 prevents the growth of endothelial cells, and its systemic administration inhibits the growth of primary carcinomas in mice. Angiostatin Kringles 1-3 segment has a larger inhibitory activity than the Angiostatin kringles 1-4 fragment. The protease-activated angiostatin kringles 1-5 is the most potent plasminogen fragment with over 50 times larger endothelial cell specific inhibitory activity. Angiostatin kringles 1-5 systemic administration inhibits growth of fibrosarcoma and significantly reduces neovascularization.
      Angiostatin is an angiogenesis inhibitor in mouse serum and urine. Angiostatin is a 38 kDa protein fragment of the plasminogen composed of the 1st 4 kringle domains of plasminogen. Angiostatin K1-4 is also named plasminogen kringles 1-4 and PK1-4.
      Angiostatin protein is manufactured by the protelytic cleavage of plasminogen by a serine protease from several prostate carcinoma cell lines. The manufacturing of angiostatin by pancreatic cancer cells can be inhibited by TGF-beta 1 along with plasminogen activator inhibitor type-1 (PAI1).

    • Physical Appearance

      Sterile Filtered lyophilized powder.

    • Stability

      Lyophilized Angiostatin Kringles 1-4 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Angiostatin Kringles1-4 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.

    • Solubility

      It is recommended to reconstitute the lyophilized Angiostatin K1-4 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    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.

    Angiostatin K1 4 Human
  • View Data Sheet

    Name :

    SGTA Human

    Description:

    Small Glutamine-Rich Tetratricopeptide Repeat-Containing Protein Alpha Human Recombinant

    alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.

    Product # :

    PRO-807

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    Description

    SGTA Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 321 amino acids (1-313 a.a.) and having a molecular mass of 35.1 kDa. SGTA protein is fused to a 8 amino acid His-Tag at C-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    SGTA Human solution containing 20mM Trsi HCL pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      SGTA is a ubiquitously expressed protein that contains three TPR protein-protein interaction duplicates. SGTA takes part as a component of the androgen receptor (AR)-chaperone-cochaperone complex, functions as a cochaperone and participates in androgen signaling. SGTA binds directly to HSC70 and HSP70 and mediates their ATPase activity. SGTA gene encodes a protein that is able to interact with the chief nonstructural protein of parvovirus H-1 and 70-kDa heat shock cognate. In addition, SGTA interacts with Vpu and Gag from HIV-1, SARS-CoV accessory protein 7a, DNAJC5 and DNAJC5B. Since this transcript is expressed universally in several tissues, SGTA serves a housekeeping function. While being involved in apoptosis and androgen signaling, SGTA is a possible molecule for polycystic ovary syndrome, a disorder characterized by androgen excess, obesity and menstrual disturbances.

    • Synonyms

      alphaSGT, hSGT, SGT, Vpu-binding protein, UBP, Small glutamine-rich tetratricopeptide repeat-containing protein alpha, Alpha-SGT, SGT1.

    • 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.

    • Amino Acid Sequence

      MDNKKRLAYA IIQFLHDQLR HGGLSSDAQE SLEVAIQCLE TAFGVTVEDS DLALPQTLPE IFEAAATGKE MPQDLRSPAR TPPSEEDSAE AERLKTEGNE QMKVENFEAA VHFYGKAIEL NPANAVYFCN RAAAYSKLGN YAGAVQDCER AICIDPAYSK AYGRMGLALS SLNKHVEAVA YYKKALELDP DNETYKSNLK IAELKLREAP SPTGGVGSFD IAGLLNNPGF MSMASNLMNN PQIQQLMSGM ISGGNNPLGT PGTSPSQNDL ASLIQAGQQF AQQMQQQNPE LIEQLRSQIR SRTPSASNDD QQELEHHHHH H.

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    Sgta Human
  • View Data Sheet

    Name :

    STEAP4 Human

    Description:

    STEAP Family Member 4 Human Recombinant

    DKFZp666D049, FLJ23153, STAMP2, TIARP, TNFAIP9, Six-transmembrane epithelial antigen of prostate 4, SixTransMembrane protein of prostate 2, Tumor necrosis factor, alpha-induced protein 9.

    Product # :

    PRO-1893

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    Description

    STEAP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-152 a.a) and having a molecular mass of 20.6kDa.STEAP4 is fused to a 36 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    STEAP4 protein solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.4M UREA and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      STEAP Family Member 4 (STEAP4) is a member of the STEAP (six transmembrane epithelial antigen of prostate) family, resides in the golgi apparatus. STEAP4 act as a metalloreductase which has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+),using NAD(+) as acceptor. According to studies in mice and human it is possible that STEAP4 may involve in adipocyte development and metabolism, and also contribute to the normal biology of the prostate cell.

    • Synonyms

      DKFZp666D049, FLJ23153, STAMP2, TIARP, TNFAIP9, Six-transmembrane epithelial antigen of prostate 4, SixTransMembrane protein of prostate 2, Tumor necrosis factor, alpha-induced protein 9.

    • Physical Appearance

      Sterile Filtered clear 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.

    • Amino Acid Sequence

      MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSMEKT CIDALPLTMN SSEKQETVCI FGTGDFGRSL GLKMLQCGYS VVFGSRNPQK TTLLPSGAEV LSYSEAAKKS GIIIIAIHRE HYDFLTELTE VLNGKILVDI SNNLKINQYP ESNAEYLAHL VPGAHVVKAF NTISAWALQS GALDASRQ.

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    Steap4 Human
  • View Data Sheet

    Name :

    Resistin Human, His

    Description:

    Resistin Human Recombinant, His Tag

    Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    Product # :

    CYT-256

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    Description

    Resistin Human Recombinant produced in E.Coli is a single, non-glycosylated, Polypeptide chain containing a 92 amino acids fragment (17-108) of the mature Human Resistin, having a total molecular mass of 14.23kDa and fused with a 4.5kDa amino-terminal hexahistidine tag. The Resistin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Resistin protein solution is supplied in 20mM Tris-HCl pH 8.0, 5mM EDTA and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Resistin, a product of the RSTN gene, is a peptide hormone belonging to the class of cysteine-rich secreted proteins which is termed the RELM family, and is also described as ADSF (Adipose Tissue- Specific Secretory Factor) and FIZZ3 (Found in Inflammatory Zone). Human resistin contains 108 amino acids as a prepeptide, and its hydrofobic signal peptide is cleaved before its secretion. Resistin circulates in human blood as a dimeric protein consisting of two 92 amino acid polypeptides, which are disulfide-linked via Cys26.
      Resistin may be an important link between obesity and insulin resistance. Mouse resistin, specifically produced and secreted by adipocyte, acts on skeletal muscle myocytes, hepatocytes and adipocytes themselves so that it reduces their sensitivity to insulin. Steppan et al. have suggested that resistin suppresses the ability of insulin to stimulate glucose uptake. They have also suggested that resistin is present at elevated levels in blood of obese mice, and is down regulated by fasting and antidiabetic drugs. Way et al., on the other hand, have found that resistin expression is severly suppressed in obesity and is stimulated by several antidiabetic drugs.
      Other studies have shown that mouse resistin increases during the differentiation of adipocytes, but it also seems to inhibit adipogenesis. In contrast, the human adipogenic differentiation is likely to be associated with a down regulation of resistin gene expression.

    • Synonyms

      Cysteine-rich secreted protein FIZZ3, Adipose tissue-specific secretory factor, ADSF, C/EBP-epsilon-regulated myeloid-specific secreted cysteine-rich protein, Cysteine-rich secreted protein A12-alpha-like 2, RSTN, XCP1, RETN1, MGC126603, MGC126609.

    • 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.Please avoid freeze thaw cycles.

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    Resistin Human His
  • View Data Sheet

    Name :

    s100bb Human

    Description:

    s100bb Human homodimer

    Product # :

    PRO-2797

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    • More Info

    Description

    s100bb Human produced in Human brain tissue is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.

    Source

    Human brain tissue.

    Formulation

    s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.

    Purity

    Greater than 95.0% .

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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.

    • Solubility

      It is recommended to reconstitute the lyophilized s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      S100BB is not only active in mature brains but also plays a significant role during brain development. It contributes to neural progenitor cell proliferation, neuronal migration, and differentiation. Studies have suggested that alterations in S100BB expression during development might influence the wiring of neural circuits, potentially impacting cognitive functions later in life. Investigating these developmental aspects of S100BB provides essential insights into neurogenesis and brain architecture.

      Implications in Neurological Disorders:

      Research has indicated potential links between abnormal S100BB levels and neurological disorders. Elevated S100BB levels have been observed in conditions such as traumatic brain injury, stroke, and neurodegenerative diseases. Its release into the bloodstream following CNS damage has positioned S100BB as a biomarker for CNS injury. Additionally, studies have explored its involvement in neuroinflammation and synaptic dysfunction, offering a glimpse into its role in diseases like Alzheimer’s and Parkinson’s.

      Conclusion:

      S100BB, once regarded as a brain-specific protein, has emerged as a pivotal player in neurological signaling and development. Its intricate involvement in cellular processes within the CNS underscores its significance in understanding brain function and disorders. As research delves deeper into the regulatory mechanisms and functional implications of S100BB, it holds promise for unveiling novel therapeutic targets for neurological diseases. This study aims to shed light on the multifaceted nature of S100BB, emphasizing its crucial roles in the intricate landscape of the central nervous system.

    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.

    S100Bb Human
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