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Search results

1000 results found for “calcium binding protein”

Name

Description

Product #

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  • View Data Sheet

    Name :

    THRSP Human

    Description:

    Thyroid Hormone Responsive Human Recombinant

    Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 protein.

    Product # :

    PRO-1485

    Price :

    Quantity :

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    • source
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    Description

    THRSP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-146 a.a.) and having a molecular mass of 18.9kDa.THRSP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Thyroid Hormone Responsive (THRSP) is a member of the SPOT14 family. THRSP is similar to the gene product of S14, a rat gene whose expression is limited to liver and adipose tissue and is controlled by nutritional and hormonal factors. THRSP is expressed in liver and adipocytes, specifically in lipomatous modules. In addition It is expressed in lipogenic breast cancers, which suggests a role in controlling tumor lipid metabolism.

    • Synonyms

      Lpgp, LPGP1, S14, SPOT14, THRP, Spot 14 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. 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 MGSMQVLTKR YPKNCLLTVM DRYAAEVHNM EQVVMIPSLL RDVQLSGPGG QAQAEAPDLY TYFTMLKAIC VDVDHGLLPR EEWQAKVAGS EENGTAETEE VEDESASGEL DLEAQFHLHF SSLHHILMHL TEKAQEVTRK YQEMTGQVW.

    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.

    Thrsp Human
  • View Data Sheet

    Name :

    GDF11 Human, His

    Description:

    Growth and Differentiation factor 11 Human Recombinant, His Tag

    Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

    Product # :

    CYT-887

    Price :

    Quantity :

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    Description

    GDF11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids (299-407a.a) and having a molecular mass of 14.8kDa. GDF11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GDF11 protein solution (1mg/ml) containing 20mM Tris-HCl (pH8.0) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      GDF-11 belongs to the bone morphogenetic protein (BMP) family and the TGF-beta superfamily. GDF-11 is a central developmental factor which controls muscular and neural development. In adults, GDF-11 encourages cardiac hypertrophy reverse by the revival of cardiomyocytes.

    • Synonyms

      Growth Differentiation Factor 11, BMP11, Bone Morphogenetic Protein 11, BMP-11, GDF-11, Growth/Differentiation Factor 11, Growth/differentiation factor 11.

    • 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 MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

    • Background

      What is the molecular weight/Mw of GDF11 HUMAN, HIS Protein?
      GDF11 HUMAN, HIS Protein has a total Mw of 14.8kDa.

      What is the source or expression system of GDF11 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of GDF11 HUMAN, HIS Protein?
      GDF11 HUMAN, HIS Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of GDF11 HUMAN, HIS Protein?
      The biological functionality of GDF11 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of GDF11 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MGSNLGLDCD EHSSESRCCR YPLTVDFEAF GWDWIIAPKR YKANYCSGQC EYMFMQKYPH THLVQQANPR GSAGPCCTPT KMSPINMLYF NDKQQIIYGK IPGMVVDRCG CS.

      What applications can GDF11 HUMAN, HIS Protein be used in?
      GDF11 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for GDF11 HUMAN, HIS Protein?
      The endotoxin level is minimal, GDF11 HUMAN, HIS 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.

    Gdf11 Human His
  • View Data Sheet

    Name :

    SIVA1 Human

    Description:

    SIVA1 Human Recombinant

    Apoptosis regulatory protein Siva isoform 1, Apoptosis regulatory protein Siva, CD27-binding protein, CD27BP, SIVA, SIVA1, Siva-1, Siva-2

    Product # :

    PRO-2652

    Price :

    Quantity :

    Shipping Method :

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    SIVA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 198 amino acids (1-175 a.a.) and having a molecular mass of 21.1 kDa. SIVA1 is fused to a 23 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SIVA1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SIVA1, also referred to asApoptosis regulatory protein Siva isoform 1, is a death domain-containing proapoptotic protein. It is known as glucocorticoid-induced TNFR family-related gene, and also as an intracellular ligand of CD27, which are both members of the TNFR family expressed on lymphoid cells. There isn’t much known about the signalling pathway underlying the Siva-induced apoptosis.SIVA1 expression is modulated in multiple pathological processes.

    • Synonyms

      Apoptosis regulatory protein Siva isoform 1, Apoptosis regulatory protein Siva, CD27-binding protein, CD27BP, SIVA, SIVA1, Siva-1, Siva-2

    • 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 MGSMPKRSCP FADVAPLQLK VRVSQRELSR GVCAERYSQE VFEKTKRLLF LGAQAYLDHV WDEGCAVVHL PESPKPGPTG APRAARGQML IGPDGRLIRS LGQASEADPS GVASIACSSC VRAVDGKAVC GQCERALCGQ CVRTCWGCGS VACTLCGLVD CSDMYEKVLC TSCAMFET

    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.

    Siva1 Human
  • View Data Sheet

    Name :

    Tpc1808 Rat

    Description:

    Tropic 1808 Rat Recombinant

    Tropic 1808, Tpc1808.

    Product # :

    PRO-587

    Price :

    Quantity :

    Shipping Method :

    Room Temp Icon

    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    Tropic-1808 Rat Recombinant protein fused to N-terminal His-Tag produced in E.Coli is a single, non-glycosylated polypeptide chain containing 285 amino acids and having a molecular mass of 29.1 kDa.The Tpc1808 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Tropic-1808 was lyophilized from 1X PBS, pH 7.4.

    Purity

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

    More Info

    • Introduction

      Tropic 1808 is a candidate chemotropic factor induced by nerve injury. Tpc1808 protein, similar to NGF, could promote the expression of NF-H in a time-dependent manner. Tpc1808 is the gene related to promotion of nerve growth, and both the Tpc1808 gene and the Tpc1808 recombinant protein up-regulate the expression of NF-H in PC12 cells.

    • Synonyms

      Tropic 1808, Tpc1808.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Tpc1808 although stable 10°C for 1 week, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MSYYHHHHHHMNLAQIAALNQISNLNAIRVGQVLKVSNAAGSNNTQNTTQPS
      AGVPTNTASSTTGYTVKSGDTLSAIAAANGVSLANLLSWNNLSLQAIIYPGQKL
      TIQNANNATVTTPNAPTSTPTVMPSTNGSYTVKSGDTLYGIAAKLGTNVQTLLS
      LNGLQLSSTIYVGQVLKTTGAVAGAGTATSTPTPVTPTVSKPAAANGVSTAGLS
      AAQAAWLRTAVVDAQAATAGTGVLASVTVAQAILESGWGQSALASAPYHNF
      NLYLIKVKNTWKLMTLLLS.

    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.

    Tropic 1808 Rat
  • View Data Sheet

    Name :

    CFB-a Human

    Description:

    Complement Factor B Fragment a Human

    Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    Product # :

    PRO-2735

    Price :

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    • More Info

    Description

    CFB-a Human produced in Human Plasma having a molecular mass of 33 kDa.

    Source

    Human Plasma.

    Formulation

    CFB-a solution (1mg/ml) contains Phosphate-buffered saline, pH 7.2.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Complement Factor B, also known as CFB, encodes complement factor B which is a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Once the alternative pathway is activated it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which connects with C3b to form the alternative pathway C3 convertase. Also, Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation.

    • Synonyms

      Complement factor B (EC:3.4.21.47), C3/C5 convertase, Glycine-rich beta glycoprotein, GBG, PBF2, Properdin factor B, Complement factor B Ba fragment, Complement factor B Bb fragment, CFB, Complement Factor B, BFD, AHUS4, BF, BFD, CFAB, FB, FBI12, H2-Bf.

    • Physical Appearance

      Sterile filtered solution.

    • Stability

      CFB-a Human is stable at 4°C if entire vial will be used within 2-4 weeks. Store, frozen below -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.

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV and HBSAG.

    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.

    Cfb Protein
  • View Data Sheet

    Name :

    CETN3 Human

    Description:

    Centrin-3 Human Recombinant

    CEN3, CEN-3, CETN-3.

    Product # :

    PRO-533

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    Description

    CETN3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 187 amino acids (1-167 a.a.) and having a molecular mass of 21.7 kDa. CETN3 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    CETN3 Human 0.5mg/ml solution contains 20mM Trsi HCl pH-8, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      CETN3 comprises of 4 EF-hand calcium binding domains, and is a part of the centrin protein family. CETN3 protein is widely expressed cytoskeletal components that demonstrate increased expression during cell differentiation. CETN3 takes part in centrosome reproduction.

    • Synonyms

      CEN3, CEN-3, CETN-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

      MGSSHHHHHH SSGLVPRGSH MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD VKKADVLKIL
      KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI
      AIMTGDI.

    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.

    Cetn3 Human
  • View Data Sheet

    Name :

    PCBP1 Human

    Description:

    Poly (RC) Binding Protein 1 Human Recombinant

    Poly(rC) binding protein 1, hnRNP-E1, hnRNP-X, HNRPE1, HNRPX, Alpha-CP1, Heterogeneous nuclear ribonucleoprotein E1, Nucleic acid-binding protein SUB2.3, PCBP1.

    Product # :

    PRO-1690

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    Description

    PCBP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 186 amino acids (1-163) and having a molecular mass of 19.6 kDa.PCBP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PCBP1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PCBP1 is a single-stranded nucleic acid binding protein that binds preferentially to oligo dC. PCBP1 plays a role in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability. PCBP1 along with PCBP-2 and hnRNPK corresponds to the major cellular poly(rC)-binding protein. PCBP1 and PCBP-2 also functions as translational coactivators of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES and promotes poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure.

    • Synonyms

      Poly(rC) binding protein 1, hnRNP-E1, hnRNP-X, HNRPE1, HNRPX, Alpha-CP1, Heterogeneous nuclear ribonucleoprotein E1, Nucleic acid-binding protein SUB2.3, PCBP1.

    • 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 MGSMDAGVTE SGLNVTLTIR LLMHGKEVGS IIGKKGESVK RIREESGARI NISEGNCPER IITLTGPTNA IFKAFAMIID KLEEDINSSM TNSTAASRPP VTLRLVVPAT QCGSLIGKGG CKIKEIREST GAQVQVAGDM LPNSTERAIT IAGVPQSVTE CVKQIC.

    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.

    Pcbp1 Human
  • View Data Sheet

    Name :

    FABP3 Human, His

    Description:

    Fatty Acid Binding Protein 3 Human Recombinant, His Tag

    Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    Product # :

    PRO-668

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    Description

    FABP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids and having a molecular mass of 19.1 kDa. FABP3 is fused to a 37 amino acid His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP3 His-Tag is supplied in 20mM Tris-HCl pH 8.0 and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Recombinant Fatty Acid Binding Protein is a newly introduced plasma marker of acute myocardial infarction (AMI). The plasma kinetics of FABP (15kD) closely resemble those of myoglobin in that elevated plasma concentrations are found within 2 hours after AMI and return to normal generally within 18 to 24 hours. But the concentration of FABP in the skeletal muscle is 20 times lower than in cardiac tissue (for myoglobin the same content for cardiac and skeletal tissue), that makes FABP to be more cardiac specific than myoglobin. This makes FABP a useful biochemical marker for the early assessment or exclusion of AMI. FABP also appears to be a useful plasma marker for the estimation of myocardial infarct size.

    • Synonyms

      Fatty acid-binding protein heart, H-FABP, Heart-type fatty acid-binding protein, Muscle fatty acid-binding protein, M-FABP, Mammary-derived growth inhibitor, MDGI, FABP3, FABP11, O-FABP.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

    Fabp3 Human His
  • View Data Sheet

    Name :

    PBLD Human

    Description:

    Phenazine Biosynthesis-Like Protein Domain Containing Human Recombinant

    Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    Product # :

    PRO-010

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    Description

    PBLD Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 308 amino acids (1-288 a.a.) and having a molecular mass of 33.9kDa. The PBLD is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PBLD solution (1 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      PBLD is member of the phenazine biosynthesis-like protein (PhzF) family. PBLD which is expressed in most tissues is the only representative of the PhzF family in the human genome. PBLD participates in the MAPK signaling pathway. PBLD is involved in multiple basic cellular functions, its expression is elevated in several disease processes, including folate deficiency and hypotension.

    • Synonyms

      Phenazine biosynthesis-like domain-containing protein, MAWD-binding protein, Unknown protein 32 from 2D-page of liver tissue, PBLD, MAWBP, MAWDBP, FLJ14767, FLJ35507.

    • 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 MKLPIFIADA FTARAFRGNP AAVCLLENEL DEDMHQKIAR EMNLSETAFI RKLHPTDNFA QSSCFGLRWF TPASEVPLCG HATLASAAVL FHKIKNMNST LTFVTLSGEL RARRAEDGIV LDLPLYPAHP QDFHEVEDLI KTAIGNTLVQ DICYSPDTQK LLVRLSDVYN RSFLENLKVN TENLLQVENT GKVKGLILTL KGEPGGQTQA FDFYSRYFAP WVGVAEDPVT GSAHAVLSSY WSQHLGKKEM HAFQCSHRGG ELGISLRPDG RVDIRGGAAV VLEGTLTA.

    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.

    Pbld Human
  • View Data Sheet

    Name :

    PTPRN Human

    Description:

    Protein Tyrosine Phosphatase Receptor Type N Human Recombinant

    Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.

    Product # :

    ENZ-1162

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    Description

    Recombinant Human Protein Tyrosine Phosphatase Receptor Type N produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 46kDa. PTPRN is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.

    Source

    Sf9 insect cells.

    Formulation

    PTPRN is supplied in 50mM Sodium phosphate (pH 8.0) and 20% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein Tyrosine Phosphatase Receptor Type N (PTPRN) is a catalytically inactive protein and a major target of autoimmune response in diabetes mellitus. The long C-terminal intracellular tail covers the majority of autoantibody epitopes. PTPRN is expressed in neural, neuroendocrine and pancreatic islet cells.

    • Synonyms

      Receptor-type tyrosine-protein phosphatase-like N, R-PTP-N, Islet cell antigen 512, ICA 512, Islet cell autoantigen 3, PTP IA-2, PTPRN, ICA3, ICA512.

    • 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. Avoid multiple 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.

    Ptprn Human
  • View Data Sheet

    Name :

    SPARC Human

    Description:

    Secreted Protein Acidic & Rich in Cysteine Recombinant Human

    Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

    Product # :

    PRO-2602

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    Description

    Secreted Protein Acidic & Rich in Cysteine Human Recombinant produced in E.Coli is a single, non- glycosylated polypeptide chain containing 286 amino acids and having a molecular mass of 32.7kDa.SPARC 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 98.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by its ability to inhibit the cell growth of Mv1Lu mink lung epithelial cells is < 3.0 µg/mL, corresponding to a specific activity of > 333 IU/mg.

    More Info

    • Introduction

      SPARC, an acronym for “secreted protein, acidic and rich in cysteine”, is also known as osteonectin or BM-40. It is the founding member of a family of secreted matricellular proteins with similar domain structure. The 303 amino acid, 43 kDa protein contains a 17 aa signal sequence, an N-terminal acidic region that binds calcium, a follistatin domain containing Kazal-like sequences, and a C-terminal extracellular calcium (EC) binding domain with two EF-hand motifs. SPARC is produced by fibroblasts, capillary endothelial cells, platelets and macrophages, especially in areas of tissue morphogenesis and remodeling. SPARC shows context-specific effects, but generally inhibits adhesion, spreading and proliferation, and promotes collagen matrix formation. For endothelial cells, SPARC disrupts focal adhesions and binds and sequesters PDGF and VEGF. SPARC is abundantly expressed in bone, where it promotes osteoblast differentiation and inhibits adipogenesis.

    • Synonyms

      Osteonectin, ON, Basement-membrane protein 40, BM-40, SPARC, Secreted Protein acidic and Rich in Cysteine.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized SPARC although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Secreted Protein Acidic & Rich in Cysteine should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Amino Acid Sequence

      APQQEALPDE TEVVEETVAE VTEVSVGANP VQVEVGEFDD GAEETEEEVV AENPCQNHHC KHGKVCELDE NNTPMCVCQD PTSCPAPIGE FEKVCSNDNK TFDSSCHFFA TKCTLEGTKK GHKLHLDYIG PCKYIPPCLD SELTEFPLRM RDWLKNVLVT LYERDEDNNL LTEKQKLRVK KIHENEKRLE AGDHPVELLA RDFEKNYNMY IFPVHWQFGQ LDQHPIDGYL SHTELAPLRA PLIPMEHCTT RFFETCDLDN DKYIALDEWA GCFGIKQKDI DKDLVI.

    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.

    Sparc Protein
  • View Data Sheet

    Name :

    Protein A, 434 a.a

    Description:

    Staphylococcal Protein A 434 a.a Recombinant

    Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    Product # :

    PRO-686

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    Description

    Recombinant Staphylococcal Protein A produced in E.Coli is a non-glycosylated, Polypeptide chain containing 434 amino acids (37-469 a.a.) and having a molecular mass of 48.1 kDa. Recombinant Staphylococcal Protein A is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Protein-A protein solution contains 20mM Tris-HCl, pH-8 and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Protein A is a cell wall protein deriving from Staphylococcus aureus which exhibits unique binding properties for IgG from a variety of mammalian species and for some IgM and IgA as well. It binds with the Fc region of immunoglobulins through interaction with the heavy chain. It couples to a wide variety of reporter molecules including fluorescent dyes, enzyme markers, biotin, colloidal gold and radioactive iodine without affecting the antibody binding site. Recombinant Protein A was developed to increase the specificity of the molecule for IgG and is widely used both in research and bioprocessing. The recombinant protein A is produced by expressing a modified protein A gene in E.coli. A specific purification process with strict quality control was taken to get the recombinant protein A with the purity of more than 98% , no human IgG affinity step is used during validated fermentation and purification and devoid of bacterial contaminant found normally in native Protein A. (Free of Staphylococcus endotoxins and hemolysin).

    • Synonyms

      Immunoglobulin G-binding protein A, IgG-binding protein A, Staphylococcal protein A, SPA.

    • 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

      MAQHDEAQQN AFYQVLNMPN LNADQRNGFI QSLKDDPSQS ANVLGEAQKL NDSQAPKADA QQNNFNKDQQ SAFYEILNMP NLNEAQRNGFIQSLKDDPSQ STNVLGEAKK LNESQAPKAD NNFNKEQQNA FYEILNMPNL NEEQRNGFIQ SLKDDPSQSA NLLSEAKKLN ESQAPKADNK
      FNKEQQNAFY EILHLPNLNE EQRNGFIQSL KDDPSQSANL LAEAKKLNDA QAPKADNKFN KEQQNAFYEI LHLPNLTEEQ RNGFIQSLKDDPSVSKEILA EAKKLNDAQA PKEEDNNKPG KEDNNKPGKE DNNKPGKEDG NKPGKEDNKK PGKEDNKKPG KEDNKKPGKE DGNKPGKEDN
      KKPGKEDGNG VHVVKPGDTV NDIAKANGTT ADKIAADNKL ADKNMIKPGQ ELVVDKKQPA NHADANKAQA LPET.

    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.

    Protein A 434Aa
  • View Data Sheet

    Name :

    GrpE E.Coli

    Description:

    HSP-70 Cofactor (HSP24) E.Coli Recombinant

    HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    Product # :

    HSP-014

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    Description

    GrpE Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 197 amino acids and having a molecular mass of 21.8 kDa. The GrpE is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The HSP24 protein solution contains 20mM Tris-HCl pH-8 and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by analysis by SDS-PAGE.

    More Info

    • Introduction

      GrpE , co-chaperone of E.coli, participates actively in the response to hyperosomotic and heat shock by preventing the aggregation of stress-denatured proteins in association with DnaK. This protein is the nucleotide exchange factor for DnaK and may function as a thermosensor. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.

    • Synonyms

      HSP24, HSPB25.3, HSP-70 Cofactor, Protein grpE, Heat shock protein B25.3, grpE, b2614, JW2594.

    • 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

      MSSKEQKTPE GQAPEEIIMD QHEEIEAVEP EASAEQVDPR DEKIANLEAQ LAEAQTRERD GILRVKAEME NLRRRTELDI EKAHKFALEK FINELLPVID SLDRALEVAD KANPDMSAMV EGIELTLKSM LDVVRKFGVE VIAETNVPLD PNVHQAIAMV ESDDVAPGNV LGIMQKGYTL NGRTIRAAMV TVAKAKA.

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    Grpe Ecoli
  • View Data Sheet

    Name :

    RBM11 Human

    Description:

    RNA Binding Motif Protein 11 Human Recombinant

    Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.

    Product # :

    PRO-1802

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    Description

    RBM11 Human Recombinant produced in E. coli is a single polypeptide chain containing 304 amino acids (1-281) and having a molecular mass of 34.6kDa. RBM11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The RBM11 solution (1mg/ml) contains 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

      RNA Binding Motif Protein 11 (RBM11) which contains 1 RNA recognition motif is a part of the RBM family. The RBM gene family encodes proteins with an RNA binding motif which participate in the modulation of apoptosis. RBM11 is expressed in testis, kidney, spleen, brain, spinal cord and mammary gland and can be found as 2 isoforms produced by alternative splicing.

    • Synonyms

      Splicing regulator RBM11, RNA-binding motif protein 11, RBM11.

    • 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 MGSMFPAQEE ADRTVFVGNL EARVREEILY ELFLQAGPLT KVTICKDREG KPKSFGFVCF KHPESVSYAI ALLNGIRLYG RPINVQYRFG SSRSSEPANQ SFESCVKINS HNYRNEEMLV GRSSFPMQYF PINNTSLPQE YFLFQKMQWH VYNPVLQLPY YEMTAPLPNS ASVSSSLNHV PDLEAGPSSY KWTHQQPSDS DLYQMTAPLP NSASVSSSLN HVPDLEAGPS SYKWTHQQPS DSDLYQMNKR KRQKQTSDSD SSTDNNRGNE CSQKFRKSKK KKRY.

    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.

    Rbm11 Human
  • View Data Sheet

    Name :

    BMP3 Human

    Description:

    Bone Morphogenetic protein-3 Human Recombinant

    Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    Product # :

    CYT-937

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    Description

    BMP3 Human Recombinant produced in E.coli is a non-glycosylated disulfide linked homodimer containing 2 chains of 110 amino acids and having a molecular mass of 24.8kDa.The BMP-3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BMP-3 protein was lyophilized from a 0.2µm filtered concentrated solution in 30% Acetonitrile and 0.1% TFA.

    Purity

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

    Biological Activity

    The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

    More Info

    • Introduction

      Bone Morphogenetic Protein 3 (BMP3) is one of the BMPs, some of which are members of the TGF-beta superfamily (BMP2-7). There are more than 13 BMPs, which are involved in inducing cartilage and bone formation, embryogenesis and morphogenesis of various tissues and organs. In addition, BMPs regulate the growth, differentiation, chemotaxis, and apoptosis of various cell types. Akin to most other TGF-beta family proteins, BMPs are extremely conserved across animal species. At the amino acid sequence level, mature human and rat BMP3 are 98% identical.

    • Synonyms

      Bone Morphogenetic Protein 3, Osteogenin, Bone Morphogenetic Protein 3 (Osteogenic), Bone Morphogenetic Protein 3A, BMP-3A, BMP-3, Bone Morphogenetic Protein-3, BMP3A, BMP3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BMP3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BMP-3 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 BMP3 in sterile 4mM HCl not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

    • Background

      Bone Morphogenetic Protein-3 Human Recombinant: Unveiling the Potential of a Key Regulator in Tissue Regeneration

      Abstract:

      Bone Morphogenetic Protein-3 (BMP-3) human recombinant is a critical member of the bone morphogenetic protein family, known for its role in tissue development, repair, and regeneration. This research paper provides a comprehensive analysis of BMP-3, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-3 human recombinant are proposed, shedding light on its future implications in the field of regenerative medicine.

      Introduction:

      Tissue regeneration is a complex biological process requiring precise molecular cues. BMP-3, a crucial member of the BMP family, plays a significant role in tissue development and regeneration. This paper explores the unique features of BMP-3 and presents novel approaches for its production and optimization, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-3 is a secreted protein that binds to cell surface receptors, initiating intracellular signaling cascades. It influences cell differentiation, proliferation, and extracellular matrix synthesis through both Smad-dependent and Smad-independent signaling pathways. BMP-3 signaling regulates critical processes involved in tissue regeneration, including chondrogenesis and osteogenesis.

      Production of BMP-3 Human Recombinant:

      Efficient production methodologies are essential for harnessing the therapeutic potential of BMP-3 human recombinant. Recombinant protein expression systems, such as Escherichia coli or mammalian cells, have been utilized to produce functional BMP-3. Optimization strategies, including codon optimization, signal peptide engineering, and protein folding optimization, have been employed to enhance the yield and activity of BMP-3 recombinant protein.

      Potential Therapeutic Applications:

      BMP-3 human recombinant holds significant promise in the field of regenerative medicine. It plays a crucial role in bone and cartilage regeneration, making it a potential candidate for the treatment of skeletal disorders and tissue injuries. Additionally, BMP-3 signaling influences tissue remodeling and wound healing, suggesting its broader therapeutic applications in other regenerative processes.

      Conclusion:

      BMP-3 human recombinant represents a key regulator in tissue regeneration, with immense potential in regenerative medicine. Optimizing production methodologies and further unraveling its signaling mechanisms will enhance its therapeutic applications. With its implications in bone and cartilage regeneration and its role in tissue remodeling, BMP-3 human recombinant emerges as a promising tool for promoting tissue repair and regeneration.

      What is the molecular weight/Mw of BMP3 Protein?
      BMP3 Protein has a total Mw of 24.8kDa.

      What is the source or expression system of BMP3 Protein?
      Escherichia Coli.

      What is the Purity of BMP3 Protein?
      BMP3 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP3 Protein?
      The ED50 as determined by its ability to inhibit BMP-2-induced activity in murine MC3T3- E1 cells.

      What is the amino acid sequence of BMP3 Protein?
      QWIEPRNCAR RYLKVDFADI GWSEWIISPK SFDAYYCSGA CQFPMPKSLK PSNHATIQSI VRAVGVVPGI PEPCCVPEKM SSLSILFFDE NKNVVLKVYP NMTVESCACR.

      What applications can BMP3 Protein be used in?
      BMP3 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP3 Protein?
      The endotoxin level is minimal, BMP3 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.

    Bmp3 Human
  • View Data Sheet

    Name :

    C5a Human

    Description:

    Complement Component C5a Human Recombinant

    Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

    Product # :

    PRO-2300

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    Description

    C5a Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 74 amino acids and having a molecular mass of 8.3kDa.The Human C5a is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Human C5a was lyophilized from a concentrated (1mg/ml) solution in PBS, pH 7.4.

    Purity

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

    Biological Activity

    The biological activity determined by its ability to chemoattract human monocytes using a concentration range of 1.0-10.0 ng/ml.

    More Info

    • Introduction

      Complement Component C5a (C5a) is involved in the complement system and it is encoded by the C5 gene in human. Complement C5 is cleaved into C5a and C5b. C5a has an imperative role in chemotaxis and C5b forms the 1st part of the complement membrane attack complex. Complement C5 is the 5th component of complement, which plays a central role in inflammatory and cell killing processes. C5a protein is composed of alpha and beta polypeptide chains, which are linked by a disulfide bridge. An activation peptide, C5a, which is an anaphylatoxin, which has potent spasmogenic and chemotactic activity, is derivative from the alpha polypeptide via cleavage with a convertase. The C5b macromolecular cleavage product forms a complex with the C6 complement component, and this complex is the basis for creation of the membrane attack complex, which includes supplementary complement components.

    • Synonyms

      Complement Component 5, C3 and PZP-Like Alpha-2-Macroglobulin Domain-Containing Protein 4, C5a Anaphylatoxin, Prepro-C5, CPAMD4, Anaphylatoxin C5a Analog, ECLZB, C5A, C5D, C5b, C5.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Human C5a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Human C5a should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized C5a Human in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      TLQKKIEEIA AKYKHSVVKK CCYDGACVNN DETCEQRAAR ISLGPRCIKA FTECCVVASQ LRANISHKDM QLGR.

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    C5A Human
  • View Data Sheet

    Name :

    ATF Human

    Description:

    Apo Transferrin Human

    Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    Product # :

    PRO-325

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    Description

    Human Apo Transferrin is a glycoprotein of approximately 77 kDa.

    Source

    Human serum.

    Formulation

    The protein was lyophilized from 20mM NH4HC03 solution. May contain traces of buffer salts.

    Purity

    Greater than 98.0% as determined by coomassie blue stained SDS-PAGE and Cellulose Acetate electrophoresis.

    More Info

    • Introduction

      Transferrin is the iron-transport protein of vertebrate serum and donates iron to cells through interaction with a specific membrane receptor, CD71. Transferrin appears to be indispensable for most cells growing in tissue culture.
      It is referred to frequently as a growth factor because, in analogy to other growth factor-receptor interactions, proliferating cells express high numbers of transferrin receptors, and the binding of transferrin to their receptors is needed for cells to initiate and maintain their DNA synthesis. Apart from its role as an iron transport protein transferrin acts as a cytokine and has functions that may not be related to its iron-carrying capacity.
      Human Transferrin is a crucial component for the cultivation of mammalian cells in-vitro. Human Transferrin is Critical for long-term cells growth in-vitro. Human Transferrin is used as detoxificant in media by binding contaminating metal ions. Human Transferrin is often used as a nutrient in fermentation media for recombinant protein and biopharmaceutical production. Additional common uses of Human Transferrin areMolecular weight, Affinity purification of anti-human transferrin antibodies and also as receptor mediated transfection of molecules such as DNA, into cells.

    • Synonyms

      Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, Apo Transferrin, ATF.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store the lyophilized Apo Transferrin between 2-8°C, do not freeze. Upon reconstitution Apo Transferrin should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

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

    • Human Virus Test

      Plasma from each donor has been tested and found negative for antibody to HIV-1, HIV-2, HCV, HBSAG and Syphilis.

    • Iron Content

      The Iron content was estimated by ICP and was found to be <6 ppm.

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    Apo Transferrin Human
  • View Data Sheet

    Name :

    FABP12 Human

    Description:

    Fatty Acid Binding Protein-12 Human Recombinant

    Fatty acid-binding protein 12, FABP12.

    Product # :

    PRO-738

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    Description

    FABP12 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 164 amino acids (1-140 a.a) and having a molecular mass of 18kDa.FABP12 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP12 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      FABP12 is a member of the calycin superfamily and fatty-acid binding protein (FABP) family. The FABPs are a family of carrier proteins for fatty acids and other lipophilic substances for example eicosanoids and retinoids. These proteins are believed to enable the transfer of fatty acids between extra- and intracellular membranes. FABP12 has a role in lipid transport. FABP12 is expressed in several retinoblastoma cell lines. FABP12 has not been detected in fetal tissues.

    • Synonyms

      Fatty acid-binding protein 12, FABP12.

    • 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 MGSHMIDQLQ GTWKSISCEN SEDYMKELGI GRASRKLGRL AKPTVTISTD GDVITIKTKS IFKNNEISFK LGEEFEEITP GGHKTKSKVT LDKESLIQVQ DWDGKETTIT RKLVDGKMVV ESTVNSVICT RTYEKVSSNS VSNS.

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    Fabp12 Human
  • View Data Sheet

    Name :

    BLyS Human, Plant

    Description:

    BAFF (BLyS) Human Recombinant, Plant

    BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    Product # :

    CYT-054

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    Description

    BAFF human Recombinant produced in Nicotiana benthamiana plant is a single glycosilated polypeptide chain containing 151 amino acids fragment (134-285).BAFF (C830H1277N223O242S5) is fused to a 10-His-tag at the N-terminal having the total molecular mass of 18-20kDa and purified by standard chromatographic techniques.

    Source

    Nicotiana benthamiana plant

    Formulation

    Lyophilized from 1mg/ml solution in 20 mM PBS buffer pH 7 and 0.2 M NaCl.

    Purity

    Greater than 97.0% as determined by Analysis by SDS-PAGE.

    Biological Activity

    The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.
    *activity results may vary with PBMC donors.
    ED50 ? 50ng/ml

    More Info

    • Introduction

      BAFF binds to tnfrsf13b/taci and tnfrsf17/bcma. Tnfsf13/april binds to the same 2 receptors, together, they form a 2 ligands -2 receptors pathway involved in the stimulation of b- and t-cell function and the regulation of humoral immunity.A third b-cell specific baff-receptor (baffr/br3) promotes the survival of mature b-cells and the b-cell response.
      B Lymphocyte Stimulator functions as a potent B-cell growth factor in costimulation assays.
      Administration of BAFF Human recombinant to mice disrupts splenic B-cell and T-cell zones and results in elevated levels of serum immunoglobulin.

    • Synonyms

      BAFF, BLYS, CD257, TALL1, THANK, ZTNF4, TALL-1, TNFSF20, TNFSF13B, B-cell Activating Factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized BAFF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BAFF 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 BAFF in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

    • Background

      What is the molecular weight/Mw of BLYS Protein?
      BLYS Protein has a total Mw of 19kDa.

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

      What is the Purity of BLYS Protein?
      BLYS Protein is >97% pure as determined by SDS-PAGE.

      What is the Biological Activity of BLYS Protein?
      The activity is determined by dose-dependent stimulation of proliferation B cell from Human PBMC. Cell proliferation was measured by MTT method.

      What is the amino acid sequence of BLYS Protein?
      HHHHHHHHHH AVQGPEETVT QDCLQLIADS ETPTIQKGSY TFVPWLLSFK RGSALEEKEN KILVKETGYF FIYGQVLYTD KTYAMGHLIQ RKKVHVFGDE LSLVTLFRCI QNMPETLPNN SCYSAGIAKL EEGDELQLAI PRENAQISLD GDVTFFGALK LL

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

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

    Baff Human Plant
  • View Data Sheet

    Name :

    CRKL Human

    Description:

    V-crk Sarcoma Virus CT10 Oncogene Homolog (Avian)-Like Human Recombinant

    Crk-like protein, CRKL.

    Product # :

    PRO-063

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    Description

    CRKL Human Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 323 amino acids (1-303 a.a.) and having a molecular mass of 35.9kDa (Molecular size on SDS-PAGE will appear higher). The CRKL is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRKL solution (1 mg/ml) 20mM Tris-HCl buffer (pH 8.0), 10% glycerol, 2mM DTT and 0.1M NaCl.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Crk-like protein (CRKL) is a protein kinase containing SH2 and SH3 (src homology) domains which activates the RAS and JUN kinase signaling pathways and transforms fibroblasts in a RAS-dependent manner. CRKL is a substitute of the BCR-ABL tyrosine kinase, it also has a role in fibroblast transformation by BCR-ABL, and has oncogenic potential.

    • Synonyms

      Crk-like protein, CRKL.

    • 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 MSSARFDSSD RSAWYMGPVS RQEAQTRLQG QRHGMFLVRDSSTCPGDYVL SVSENSRVSH YIINSLPNRR FKIGDQEFDH LPALLEFYKI HYLDTTTLIE PAPRYPSPPM GSVSAPNLPT AEDNLEYVRT LYDFPGNDAE DLPFKKGEIL VIIEKPEEQW WSARNKDGRV GMIPVPYVEK LVRSSPHGKH GNRNSNSYGI PEPAHAYAQP QTTTPLPAVS GSPGAAITPL PSTQNGPVFA KAIQKRVPCA YDKTALALEV GDIVKVTRMN INGQWEGEVN GRKGLFPFTH VKIFDPQNPD ENE.

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    CRKL Human
  • View Data Sheet

    Name :

    FABP4 Human, His

    Description:

    Fatty Acid Binding Protein 4 Human Recombinant, His Tag

    Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    Product # :

    PRO-566

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    Description

    FABP4 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 132 amino acids and having a molecular mass of 18 kDa. FABP4 is fused to His tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    FABP4 His-Tag is supplied in 20mM Tris HCL pH=8, 0.5mM DTT and 50% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      Adipocyte fatty acid binding protein FABP4 is a 15 kDa member of the intracellular fatty acid binding protein (FABP) family, which is known for the ability to bind fatty acids and related compounds (bile acids or retinoids) in an internal cavity. FABP4 is expressed in a differentiation-dependent fashion in adipocytes and is a critical gene in the regulation of the biological function of these cells.
      In mice, targeted mutations in FABP4 provide significant protection from hyperinsulinemia and insulin resistance in the context of both dietary and genetic obesity. Adipocytes obtained from FABP4-deficient mice also have reduced efficiency of ipolysis in vitro and in vivo, and these mice exhibited moderately improved systemic dyslipidemia. Recent studies also demonstrated FABP4 expression in macrophages upon differentiation and activation. In these cells, FABP4 modulates inflammatory responses and cholesterol ester accumulation, and total or macrophage-specific FABP4 deficiency confers dramatic protection against atherosclerosis in the apoE-/- mice. These results indicate a central role for FABP4 in the development of major components of the metabolic syndrome through its distinct actions in adipocytes and macrophages.

    • Synonyms

      Fatty acid-binding protein adipocyte, AFABP, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, ALBP, A-FABP, FABP4.

    • Physical Appearance

      Sterile Filtered colorless liquid formulation.

    • 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.

    Fabp4 Human His
  • View Data Sheet

    Name :

    CSNK2B Protein

    Description:

    Casein Kinase 2b Human Recombinant

    Casein kinase II subunit beta, CK II beta, Phosvitin, G5a, CK2B, CK2N, CSK2B, MGC138222, MGC138224.

    Product # :

    PKA-223

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    Description

    CSNK2B Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 215 amino acids and having a total molecular mass of 24.9kDa. CK2 beta is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CSNK2B protein (1 mg/ml) contains 20mM Tris-HCl pH 8.0, 200mM NaCl, 1mM DTT, 1mM EDTA, 1uM leupeptin and 40% glycerol.

    Purity

    Greater than 95.0% as determinedAnalysis by SDS-PAGE.

    More Info

    • Introduction

      Casein Kinase 2 also called CK2 (also called PKCK2) is a ubiquitous Ser/Thr kinase expressed in all eukaryotes. CK2 is a tetramer composed of two catalytic kinase domains, alpha subunits, and two identical regulatory beta subunits. It has been implicated in cell cycle control, DNA repair, regulation of the circadian rhythm, and other cellular processes. The beta subunit itself does not have kinase activity, but confers stability to the CK2 alpha subunit and is involved in activity and substrate specificity.

    • Synonyms

      Casein kinase II subunit beta, CK II beta, Phosvitin, G5a, CK2B, CK2N, CSK2B, MGC138222, MGC138224.

    • 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). Please avoid freeze-thaw cycles.

    • Amino Acid Sequence

      MSSSEEVSWI SWFCGLRGNE FFCEVDEDYI QDKFNLTGLN EQVPHYRQAL DMILDLEPDE ELEDNPNQSD LIEQAAEMLY GLIHARYILT NRGIAQMLEK YQQGDFGYCP RVYCENQPML
      PIGLSDIPGE AMVKLYCPKC MDVYTPKSSR HHHTDGAYFG TGFPHMLFMV HPEYRPKRPA NQFVPRLYGF KIHPMAYQLQ LQAASNFKSP VKTIR.

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    Csnk2B Human
  • View Data Sheet

    Name :

    Prelamin-A

    Description:

    Prelamin-A Recombinant

    Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    Product # :

    PRO-689

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    Description

    Recombinant Prelamin-A is a 74kDa precursor of the nuclear lamin A protein. Prelamin-A is a structural component of the nuclear lamina and it is encoded by lamin A/C gene (LMNA). Due to the presence of a CAAX box sequence at carboxyl terminus, Prelamin-A in vivo goes through a serial of post-translational modifications, resulting in the farnesylation of the cysteine thiol, removal of the AAX tripeptide, carboxyl-methylation of the cysteinyl carboxy group and proteolysis of 18 C-terminal amino acids residues that lead to mature lamin A. Diverse mutations in the lamin A/C gene are associated with different deseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familial partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. Recombinant human prelamin A is fused to a 6 Histidine tag at the N-terminus.

    Source

    Escherichia Coli.

    Formulation

    The Prelamin-A solution (0.1mg/ml) contains 10% Glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Prelamin-A/C, LMNA, LMN1, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.

    • 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

      HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
      EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
      RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
      QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
      LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
      RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
      TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
      KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
      WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
      RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRSYL
      LGNSSPRTQSPQNCSIM

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    Prelamin A
  • View Data Sheet

    Name :

    MAPT Human 383a.a.

    Description:

    Microtubule-Associated Protein Tau 383 a.a. Human Recombinant

    Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    Product # :

    PRO-012

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    • source
    • formulation
    • purity
    • More Info

    Description

    MAPT Human Recombinant (Isoform 3) fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 403 amino acids (1-383 a.a.) and having a molecular mass of 42.1kDa (Molecular size on SDS-PAGE will appear higher). The MAPT is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      MAPT is a neuronal microtubule associated protein localized mostly on axons.
      MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain.

    • Synonyms

      Microtubule-associated protein tau, Neurofibrillary tangle protein, Paired helical filament-tau, PHF-tau, MAPT, MAPTL, MTBT1, TAU, MSTD, PPND, DDPAC, MTBT2, FTDP-17, FLJ31424, MGC138549.

    • 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).Please prevent freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQII NKKLDLSNVQ SKCGSKDNIK HVPGGGSVQI VYKPVDLSKV TSKCGSLGNI HHKPGGGQVE VKSEKLDFKD RVQSKIGSLD NITHVPGGGN KKIETHKLTF RENAKAKTDH GAEIVYKSPV VSGDTSPRHL SNVSSTGSID MVDSPQLATL ADEVSASLAK QGL.

    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.

    Mapt Human 383Aa
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