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Search results

1000 results found for “Dickkopf-Related Protein”

Name

Description

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  • View Data Sheet

    Name :

    RAD1 Human

    Description:

    RAD1 Human Recombinant

    RAD-1, HRAD1, REC1, Cell cycle checkpoint protein RAD1, hRAD1, EC=3.1.11.2, DNA repair exonuclease rad1 homolog, Rad1-like DNA damage checkpoint protein.

    Product # :

    PRO-868

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    Description

    RAD1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-282 a.a.) and having a molecular mass of 33.9 kDa. The RAD1 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    RAD1 Human solution containing 20mM Tris pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      RAD1 is part of a heterotrimeric cell cycle checkpoint complex, recognized as the 9-1-1 complex, that is activated to stop cell cycle progression in reaction to DNA damage or incomplete DNA replication. RAD1 complex withholds the Rad9 and Hus1 proteins and takes part in cellular responses to DNA damage, by associating with Rad17 and several components of the PCNA-loading heteropentamer, replication factor C. RAD1 takes part in DNA repair and recruited to DNA lesion upon damage by the RAD17-replication factor C (RFC) clamp loader complex. RAD1 takes part as a sliding clamp platform on DNA for several proteins that play a role in long-patch base excision repair (LP-BER). RAD1 complex stimulates DNA polymerase beta (POLB) activity by raising its affinity for the 3''-OH end of the primer-template and stabilizes POLB to those sites where LP-BER proceeds.

    • Synonyms

      RAD-1, HRAD1, REC1, Cell cycle checkpoint protein RAD1, hRAD1, EC=3.1.11.2, DNA repair exonuclease rad1 homolog, Rad1-like DNA damage checkpoint protein.

    • 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 MPLLTQQIQD EDDQYSLVAS LDNVRNLSTI LKAIHFREHA TCFATKNGIK VTVENAKCVQ ANAFIQAGIF QEFKVQEESV TFRINLTVLL DCLSIFGSSP MPGTLTALRM CYQGYGYPLM LFLEEGGVVT VCKINTQEPE ETLDFDFCST NVINKIILQS
      EGLREAFSEL DMTSEVLQIT MSPDKPYFRL STFGNAGSSH LDYPKDSDLM EAFHCNQTQV NRYKISLLKP STKALVLSCK VSIRTDNRGF LSLQYMIRNE DGQICFVEYY CCPDEEVPES ES.

    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.

    Rad1 Human
  • View Data Sheet

    Name :

    VEGF Mouse, Yeast

    Description:

    Vascular Endothelial Growth Factor Mouse Recombinant, Yeast

    Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    Product # :

    CYT-1124

    Price :

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    Description

    Vascular Endothelial Growth Factor Mouse Recombinant produced in yeast is a disulfide-linked homodimer consisting of 2x165 amino acid polypeptide chains, having a molecular mass of approximately 40.0kDa each.VEGF is purified by proprietary chromatographic techniques.

    Source

    Saccharomyces cerevisiae

    Formulation

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

    Purity

    Greater than 97.0% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    The ED50 as determined by a cell proliferation assay using human umbilical vein endothelial cells(HUVEC) is 1.0-5.0 ng/ml.

    More Info

    • Introduction

      Vascular endothelial growth factor is an important signaling protein involved in both angiogenesis and vasculogenesis.VEGF activity has been mostly studied on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g. stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells ).VEGF mediates increased vascular permeability, induces angiogenesis, vasculogenesis and endothelial cell growth, promotes cell migration, and inhibits apoptosis. In vitro, VEGF has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor.
      Elevated levels of VEGF is linked to POEMS syndrome, also known as Crow-Fukase syndrome. Mutations in VEGF have been associated with proliferative and nonproliferative diabetic retinopathy.

    • Synonyms

      Vascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGF, MGC70609.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      MAPTTEGEQK SHEVIKFMDV YQRSYCRPIE TLVDIFQEYP DEIEYIFKPS CVPLMRCAGC CNDEALECVP TSESNITMQI MRIKPHQSQH IGEMSFLQHS RCECRPKKDR TKPEKHCEPC SERRKHLFVQ DPQTCKCSCK NTDSRCKARQ LELNERTCRC DKPRR.

    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.

    Vegf Mouse Protein
  • View Data Sheet

    Name :

    CCL28 Human, His

    Description:

    Mucosae-Associated Epithelial Chemokine Human Recombinant (CCL28), His Tag

    MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    Product # :

    CHM-366

    Price :

    Quantity :

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    • description
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    • formulation
    • purity
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    Description

    CCL28 Human Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 126 amino acids (23-127 a.a.) and having a molecular mass of 14.3 kDa. The CCL28 is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CCL28 protein contains 10mM Sodium Citrate pH3.5 and 10% Glycerol.

    Purity

    Greater than 90% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      CCL28 is part of the subfamily of small cytokine CC genes. CCL28 shows chemotactic activity for resting CD4 or CD8 T cells and eosinophils. CCL28 binds to chemokine receptors CCR3 and CCR10. CCL28 is involved in the physiology of extracutaneous epithelial tissues, including diverse mucosal organs. CCL28 mediates mucosal immunity in HIV exposure and infection. CCL28 is involved in the pathogenesis of inflammatory skin diseases.
      Human CCL28 cDNA encodes a 127 amino acid residue precursor protein with a putative 22 amino acid residue signal peptide that is cleaved to produce the 105 amino acid residue mature protein. Human and mouse CCL28 are highly conserved, sharing 83% amino acid identity in their mature regions. CCL28 shares the most homology with CCL27/CTACK. Human and mouse CCL28 RNA expression was found to be highest in normal and pathologic colon with the protein being expressed by epithelial cells. Human CCL28 RNA was also present in normal and asthmatic lung tissues.

    • Synonyms

      MEC, CCK1, SCYA28, MGC71902, CCL28, C-C motif chemokine 28, Small-inducible cytokine A28, Mucosae-associated epithelial chemokine, Protein CCK1.

    • 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 MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

    • Background

      What is the molecular weight/Mw of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein has a total Mw of 14.3kDa.

      What is the source or expression system of CCL28 HUMAN, HIS Protein?
      Escherichia Coli.

      What is the Purity of CCL28 HUMAN, HIS Protein?
      CCL28 HUMAN, HIS Protein is > 90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CCL28 HUMAN, HIS Protein?
      The biological functionality of CCL28 HUMAN, HIS Protein will be determined in the future.

      What is the amino acid sequence of CCL28 HUMAN, HIS Protein?
      MGSSHHHHHH SSGLVPRGSH MILPIASSCC TEVSHHISRR LLERVNMCRI QRADGDCDLA AVILHVKRRR ICVSPHNHTV KQWMKVQAAK KNGKGNVCHR KKHHGKRNSN RAHQGKHETY GHKTPY.

      What applications can CCL28 HUMAN, HIS Protein be used in?
      CCL28 HUMAN, HIS Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CCL28 HUMAN, HIS Protein?
      The endotoxin level is minimal, CCL28 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.

    Ccl28 Human His
  • View Data Sheet

    Name :

    ENSA Human

    Description:

    Endosulfine Alpha Human Recombinant

    ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.

    Product # :

    PRO-772

    Price :

    Quantity :

    Shipping Method :

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    • description
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    Description

    ENSA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 141 amino acids (1-121 a.a.) and having a molecular weight of 15.5kDa. The ENSA is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The Endosulfine Alpha protein solution contains 20mM Tris, pH-8, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      ENSA is an endogenous ligand for sulfonylurea receptor. ENSA reduces K(ATP) channel currents by inhibiting sulfonylurea from binding to the receptor and thus stimulates insulin secretion. Endosulfine Alpha is part of a conserved cAMP-regulated phosphoprotein (ARPP) family. Endosulfine Alpha is an endogenous ligand for the sulfonylurea receptor, ABCC8/SUR1. Endosulfine Alpha is an endogenous regulator of KATP channels. ENSA modulates insulin secretion through the interaction with KATP channel. ENSA is a candidate gene for type 2 diabetes. ENSA is expressed in a wide range of tissues including muscle, brain, and endocrine tissues.

    • Synonyms

      ARPP-19e, Alpha endosulfine isoform 3, Alpha-endosulfine, ENSA, MGC4319, MGC8394, MGC78563.

    • 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 MSQKQEEENP AEETGEEKQD TQEKEGILPE RAEEAKLKAK YPSLGQKPGG SDFLMKRLQK GQKYFDSGDY NMAKAKMKNK QLPSAGPDKN LVTGDHIPTP QDLPQRKSSL VTSKLAGGQV E.

    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.

    Ensa Human
  • View Data Sheet

    Name :

    Leptin-B Tilapia

    Description:

    Leptin-B Tilapia Recombinant

    Product # :

    CYT-1110

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    Description

    Leptin-B Tilapia Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 152 amino acids and having a molecular mass of 15,243 Dalton. The Leptin-B Tilapia is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing NaHCO3 at 1:2 salt: protein ratio.

    Purity

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

    Biological Activity

    Tilapia leptins were found to be biologically active in promoting proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor, but their activity was lower than that of mammalian leptin. Furthermore, the Tilapia leptins were biologically active in promoting STAT‐LUC activation in COS7 cells transfected with Tilapia leptin receptor but not in cells transfected with human leptin receptor. Tilapia Leptin A was more active than Tilapia Leptin B.

    More Info

    • Introduction

      Leptin is a protein hormone. It is mainly produced in adipose cells that regulate energy homeostasis by restraining hunger. Leptin ties to nuclear receptors in the hypothalamus (arcuate nucleus). Similar to insulin resistance in type II diabetes, in obesity there is a decrease in the sensitivity towards leptin, ending in a failure to identify satiety, even in high levels of energy stores or leptin itself. Full-length cDNA encoding 2 leptin sequences (tLepA and tLepB) and 1 leptin receptor sequence (tLepR) exists in tilapia (Oreochromis niloticus). The full-length cDNA of tLepR is 3423 bp, encoding a protein of 1140 amino acid which contained all functionally important domains conserved among vertebrate leptin receptors. The cDNAs of tLepA and tLepB are 486 bp and 459 bp in length, encoding proteins of 161 aa and 152 aa, respectively. The three-dimensional structures of tLepA and tLepB demonstrates strong conservation of tertiary structure with that of human leptin comprised of 4 helixes.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin-B Tilapia although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leptin-B Tilapia 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 Leptin-B Tilapia in sterile water or 0.4% NaHCO3 adjusted to pH 8-9, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The first six N-terminal amino acids of recombinant Tilapia leptin B are Ala-Leu-Leu-Thr-Lys-Gly.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.19 for 1 mg/ml Leptin-B Tilapia as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the DNAman computer analysis program of protein sequences.

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    Leptin B
  • 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 :

    EMAP II Human

    Description:

    Endothelial-Monocyte Activating Polypeptide II Human Recombinant

    AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    Product # :

    CYT-607

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    Description

    EMAP-II Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 166 amino acids and having a molecular mass of 18.3 kDa. The EMAP-II is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution in water containing 20mM sodium Phosphate buffer pH=7.5 and 130mM sodium chloride.

    Purity

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

    Biological Activity

    Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

    More Info

    • Introduction

      EMAP-II also called SCYE1 is a tumor derived cytokine that plays a role in a wide variety of activities on endothelial cells, monocytes and neutrophils. EMAP-II inhibits endothelial cell proliferation, vasculogenesis, neovessel formation, and can induce apoptosis. It is also chemotactic towards neutrophils and monocytes and induces myeloperoxidase activity from neutrophils. EMAP-II clinical value is inhibiting angiogenesis of vascular beds and suppressing the growth of primary and secondary tumors with no affect to normal tissues. SCYE1is specifically induced by apoptosis, and it is involved in the control of angiogenesis, inflammation, and wound healing. The release of this SCYE1 renders the tumor-associated vasculature sensitive to tumor necrosis factor. The precursor protein is identical to the p43 subunit, which is associated with the multi-tRNA synthetase complex, and it modulates aminoacylation activity of tRNA synthetase in normal cells. EMAP-2 plays a role in in the stimulation of inflammatory responses after proteolytic cleavage in tumor cells.

    • Synonyms

      AIMP1, EMAP2, EMAP-2, EMAPII, SCYE1, Multisynthetase complex auxiliary component p43, Endothelial monocyte-activating polypeptide 2, EMAP-II, p43.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

    • Background

      What is the molecular weight/Mw of EMAP II HUMAN Protein?
      EMAP II HUMAN Protein has a total Mw of 18.3kDa.

      What is the source or expression system of EMAP II HUMAN Protein?
      Escherichia Coli.

      What is the Purity of EMAP II HUMAN Protein?
      EMAP II HUMAN Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of EMAP II HUMAN Protein?
      Determined by the apoptotic effect on MCF-7 cells using a concentration of 20-30 ng/ml.

      What is the amino acid sequence of EMAP II HUMAN Protein?
      SKPIDVSRLD LRIGCIITAR KHPDADSLYV EEVDVGEIAP RTVVSGLVNH VPLEQM QNRM VILLCNLKPA KMRGVLSQAM VMCASSPEKI EILAPPNGSV PGDRITFDAF PGEPDKELNP KKKIWEQIQP DLHTNDECVA TYKGVPFEVK GKGVCRAQTM SNSGIK.

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

      What is the endotoxin level for EMAP II HUMAN Protein?
      The endotoxin level is minimal, EMAP II HUMAN 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.

    Emap Ii
  • View Data Sheet

    Name :

    SPARC Human, Sf9

    Description:

    Secreted Protein Acidic & Rich in Cysteine Human Recombinant, Sf9

    SPARC, Basement-membrane protein 40, BM-40, Osteonectin, ON, Secreted protein acidic and rich in cysteine, OI17.

    Product # :

    PRO-2623

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    Description

    SPARC Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 295 amino acids (18-303 a.a) and having a molecular mass of 33.8kDa.SPARC is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    SPARC protein solution (0.5mg/ml) Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      SPARC protein, or secreted protein acidic and rich in cysteine, or osteonectin or basement-membrane protein 40 is a protein that is coded by the SPARC gene in humans. It is a glycoprotein located in bones, that binds to calcium. The osteonectin is secreted from osteoblasts cells when boas are formed, mineralized and promotes the formation and creation of mineral crystals. Asides from calcium, it has been shown that this protein can also bind to collagen.

    • Synonyms

      SPARC, Basement-membrane protein 40, BM-40, Osteonectin, ON, Secreted protein acidic and rich in cysteine, OI17.

    • 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

      ADPAPQQEAL PDETEVVEET VAEVTEVSVG ANPVQVEVGE FDDGAEETEE EVVAENPCQN
      HHCKHGKVCE LDENNTPMCV CQDPTSCPAP IGEFEKVCSN DNKTFDSSCH FFATKCTLEG
      TKKGHKLHLD YIGPCKYIPP CLDSELTEFP LRMRDWLKNV LVTLYERDED NNLLTEKQKL
      RVKKIHENEK RLEAGDHPVE LLARDFEKNY NMYIFPVHWQ FGQLDQHPID GYLSHTELAP
      LRAPLIPMEH CTTRFFETCD LDNDKYIALD EWAGCFGIKQ KDIDKDLVIH HHHHH

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    Sparc Human
  • View Data Sheet

    Name :

    NCF1 Human

    Description:

    Neutrophil Cytosolic Factor 1 Human Recombinant

    NCF1A, NOXO2, p47phox, SH3PXD1A .

    Product # :

    PRO-488

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    Description

    NCF1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 398 amino acids (1-390 a.a.) and having a molecular mass of 45.7 kDa. The NCF1 is fused to an 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      NCF1 is a cytosolic subunit protein of neutrophil NADPH oxidase which a
      Multi-component enzyme that is activates production of superoxide anion. NCF1, along with NCF2 and a membrane bound cytochrome b558, is necessary for activation of the latent NADPH oxidase necessary for superoxide production. Mutations in this NCF1 have been related with chronic granulomatous disease.

    • Synonyms

      NCF1A, NOXO2, p47phox, SH3PXD1A .

    • 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

      MGDTFIRHIA LLGFEKRFVP SQHYVYMFLV KWQDLSEKVV YRRFTEIYEF HKTLKEMFPI EAGAINPENR IIPHLPAPKW FDGQRAAENR QGTLTEYCST LMSLPTKISR CPHLLDFFKV RPDDLKLPTD NQTKKPETYL MPKDGKSTAT DITGPIILQT YRAIANYEKT SGSEMALSTG DVVEVVEKSE SGWWFCQMKA KRGWIPASFL EPLDSPDETE DPEPNYAGEP YVAIKAYTAV EGDEVSLLEG EAVEVIHKLL DGWWVIRKDDVTGYFPSMYL QKSGQDVSQA QRQIKRGAPP RRSSIRNAHS IHQRSRKRLS QDAYRRNSVR FLQQRRRQAR PGPQSPGSPL EEERQTQRSK PQPAVPPRPS ADLILNRCSE STKRKLASAV VEHHHHHH.

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    Ncf1 Human
  • View Data Sheet

    Name :

    CNOT7 Mouse

    Description:

    CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant

    CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    Product # :

    PRO-908

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    Description

    CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.

    • Synonyms

      CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.

    • 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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ S.

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    Cnot7 Mouse
  • View Data Sheet

    Name :

    CSTF1 Human

    Description:

    Cleavage Stimulation Factor 1 Human Recombinant

    Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    Product # :

    PRO-1170

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    Description

    CSTF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 439 amino acids (1-431 a.a) and having a molecular mass of 49.4kDa.CSTF1 is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CSTF1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 2M urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cleavage stimulation factor subunit 1 (CSTF1) is involved in the polyadenylation and 3'end cleavage of pre-mRNAs. The CSTF1 gene encodes one of three subunits which merge to produce cleavage stimulation factor (CSTF). Like the mammalian G protein beta subunits, CSTF1 contains transducin-like repeats. CSTF1 is one of the numerous factors necessary for polyadenylation and 3'-end cleavage of mammalian pre-mRNAs. CSTF1 is responsible for the interaction of CSTF with other factors to create a stable complex on the pre-mRNA.

    • Synonyms

      Cleavage stimulation factor subunit 1, CF-1 50 kDa subunit, Cleavage stimulation factor 50 kDa subunit, CSTF 50 kDa subunit, CstF-50, CSTF1, CstFp50.

    • 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

      MYRTKVGLKD RQQLYKLIIS QLLYDGYISI ANGLINEIKP QSVCAPSEQL LHLIKLGMEN DDTAVQYAIG RSDTVAPGTG IDLEFDADVQ TMSPEASEYE TCYVTSHKGP CRVATYSRDG QLIATGSADA SIKILDTERM LAKSAMPIEV MMNETAQQNM ENHPVIRTLY DHVDEVTCLA FHPTEQILAS GSRDYTLKLF DYSKPSAKRA FKYIQEAEML RSISFHPSGD FILVGTQHPT LRLYDINTFQ CFVSCNPQDQ HTDAICSVNY NSSANMYVTG SKDGCIKLWD GVSNRCITTF EKAHDGAEVC SAIFSKNSKY ILSSGKDSVA KLWEISTGRT LVRYTGAGLS GRQVHRTQAV FNHTEDYVLL PDERTISLCC WDSRTAERRN LLSLGHNNIV RCIVHSPTNP GFMTCSDDFR ARFWYRRSTT DVEHHHHHH.

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    Cstf1 Human
  • View Data Sheet

    Name :

    CGREF1 Human

    Description:

    Cell Growth Regulator With EF-Hand Domain 1 Human Recombinant

    Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 1.

    Product # :

    PRO-2154

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    Description

    CGREF1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 305 amino acids (20-301 a.a) and having a molecular mass of 32.3kDa. CGREF1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    CGREF1 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH7.4).

    Purity

    Greater than 85% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cell Growth Regulator with EF-Hand Domain 1, also known as CGREF1 is a secreted calcium ion binding protein. CGREF1 includes two EF-hand domains & both EF-hands are essential for function. CGREF1 is most likely digested extracellularly by an unfamiliar serine protease generating extremely hydrophobic bioactive peptides. CGREF1 mediates cell-cell adhesion in a calcium-dependent manner. In addition, CGREF1 is capable to inhibit growth in more than a few cell lines.

    • Synonyms

      Cell Growth Regulator With EF-Hand Domain 1, Cell Growth Regulatory Gene 11 Protein, Hydrophobestin, CGR11, Cell Growth Regulator With EF Hand Domain Protein 1, Cell Growth Regulator With EF Hand Domain 1, Cell growth regulator with EF hand domain protein 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 MGSAPKDGVT RPDSEVQHQL LPNPFQPGQE QLGLLQSYLK GLGRTEVQLE HLSREQVLLY LFALHDYDQS GQLDGLELLS MLTAALAPGA ANSPTTNPVI LIVDKVLETQ DLNGDGLMTP AELINFPGVA LRHVEPGEPL APSPQEPQAV GRQSLLAKSP LRQETQEAPG PREEAKGQVE ARRESLDPVQ EPGGQAEADG DVPGPRGEAE GQAEAKGDAP GPRGEAGGQA EAEGDAPGPR GEAGGQAEAR ENGEEAKELP GETLESKNTQ NDFEVHIVQV ENDEI.

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    Cgref1 Human
  • View Data Sheet

    Name :

    hCG Protein

    Description:

    Chorionic Gonadotropin Human

    Chorionic gonadotropin, hCG, CG.

    Product # :

    HOR-250

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    • More Info
    • Activity Assay

    Description

    Human Chorionic Gonadotropin is produced from a sterile preparation of placental glucoprotein urine of pregnant women having a total molecular mass of 36,700 Dalton. The hCG consists of 237 amino acids, a chain-92 amino acids and b chain-145 amino acids. The hCG is purified by proprietary chromatographic techniques.

    Source

    Urine of pregnant women.

    Formulation

    The hCG was lyophilized with no additives.

    Biological Activity

    The activity was found to be 5212IU/mg.

    Activity Assay

    hcg activity assay - Product image 1
    hcg bioactivity assay - Product image 2

    More Info

    • Introduction

      Human chorionic gonadotropin (hCG) is a peptide hormone produced in pregnancy, that is made by the embryosoon after conception and later by the syncytiotrophoblast(part of the placenta). Its role is to prevent the disintegration of the corpus luteumof the ovaryand thereby maintain progesterone production that is critical for a pregnancy in humans. hCG may have additional functions, for instance it is thought that it affects the immune tolerance of the pregnancy. Early pregnancy testing generally is based on the detection or measurement of hCG.

    • Synonyms

      Chorionic gonadotropin, hCG, CG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Contaminants

      Free of: HbsAg and antibodies to HIV and HCV.

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    Hcg Human
  • View Data Sheet

    Name :

    SYF2 Human

    Description:

    SYF2 RNA splicing factor Human Recombinant

    Pre-mRNA-splicing factor SYF2, CCNDBP1-interactor, p29, SYF2, CBPIN, GCIPIP, NTC31, fSAP29.

    Product # :

    PRO-969

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    Description

    SYF2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (94-243) and having a molecular mass of 20.5kDa.SYF2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The SYF2 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl, 5mM DTT and 2mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Pre-mRNA-splicing factor SYF2 (SYF2) may be involved in pre-mRNA splicing. The SYF2 protein interacts with cyclin D-type binding-protein 1, which is believed to be a cell cycle regulator at the G1/S transition. SYF2 is amply expressed in the heart, skeletal muscle and kidney and is expressed at lower levels in other tissues.

    • Synonyms

      Pre-mRNA-splicing factor SYF2, CCNDBP1-interactor, p29, SYF2, CBPIN, GCIPIP, NTC31, fSAP29.

    • 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 MGSDYEKVKL LEISAEDAER WERKKKRKNP DLGFSDYAAA QLRQYHRLTK QIKPDMETYE RLREKHGEEF FPTSNSLLHG THVPSTEEID RMVIDLEKQI EKRDKYSRRR PYNDDADIDY INERNAKFNK KAERFYGKYT AEIKQNLERG TAV.

    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.

    Syf2 Human
  • View Data Sheet

    Name :

    PKM2 Human

    Description:

    Tumor Type M2 Pyruvate Kinase Human Recombinant

    Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.

    Product # :

    PKA-339

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    Description

    PKM2 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 551 amino acids (1-531 a.a.) and having a molecular mass of 60.1kDa. The PKM2 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The PKM2 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The Specific activity is > 25,000 pmol/min/ug. 1 unit will form 1pmol of phospho(enol)pyruvate to pyruvate per minute at pH 7.5 at 37°C.

    More Info

    • Introduction

      Pyruvate kinase is a key enzyme in the glycolytic pathway. The M2 isoenzyme of pyruvate kinase is specifically expressed at high levels in tumor cells, and can be measured in plasma of patients with advanced breast cancer. The marker is useful for measuring disease activity, sensitivity to chemotherapy and recurrence.

    • Synonyms

      Pyruvate kinase isozymes M1/M2, EC 2.7.1.40, Pyruvate kinase muscle isozyme, Pyruvate kinase 2/3, Cytosolic thyroid hormone-binding protein, CTHBP, THBP1, M2PK, PKM2, PK3, PK2, PKM, TCB, OIP3, MGC3932, Tumor Type M2 Pyruvate Kinase.

    • 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 MSKPHSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSPPI TARNTGIICT IGPASRSVET LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRTATESFAS DPILYRPVAV ALDTKGPEIR TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL ISLQVKQKGA DFLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV FASFIRKASD VHEVRKVLGE KGKNIKIISK IENHEGVRRF DEILEASDGI MVARGDLGIE IPAEKVFLAQ KMMIGRCNRA GKPVICATQM LESMIKKPRP TRAEGSDVAN AVLDGADCIM LSGETAKGDY PLEAVRMQHL IAREAEAAIY HLQLFEELRR LAPITSDPTE ATAVGAVEAS FKCCSGAIIV LTKSGRSAHQ VARYRPRAPI IAVTRNPQTA RQAHLYRGIF PVLCKDPVQE AWAEDVDLRV NFAMNVGKAR GFFKKGDVVI VLTGWRPGSG FTNTMRVVPV P.

    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.

    Pkm2 Human
  • View Data Sheet

    Name :

    Borrelia Spielmanii DbpA

    Description:

    Borrelia Spielmanii Decorin Binding Protein A Recombinant

    Product # :

    BOR-026

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    Description

    Recombinant Borrelia Spielmanii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 17kDa. Borrelia Spielmanii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Borrelia Spielmanii DbpA is supplied in 20mM HEPES buffer pH-7.6, 250mM NaCl and 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Borrelia is a part of the genus of bacteria of the spirochete phylum. Borrelia causes borreliosis, which is a zoonotic, vector-borne disease transmitted mostly by ticks and some by lice, depending on the species. Of the 36 known species of Borrelia, 12 are distinguished to cause Lyme disease or borreliosis and are transmitted by ticks. The Gram-negative bacterium Borreliella spielmanii is one of the pathogens of the Borreliella burgdorferi sensu lato complex causing Lyme disease. DbpA, also known as p17 or Osp17, is a heterogeneous protein among the human pathogenic B. burgdorferi sensu lato species.

    • 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- and IgM-type human antibodies.2. Immunodot test with Lyme disease positive/negative plasma.

    • Applications

      Western blot with Lyme positive plasma.

    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.

    Borrelia Spielmanii Dbpa
  • View Data Sheet

    Name :

    SIRPG Human

    Description:

    Signal-Regulatory Protein Gamma Human Recombinant

    signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.

    Product # :

    PRO-2013

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    Description

    SIRPG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 355 amino acids (29-360 a.a.) and having a molecular mass of 39.1kDa.SIRPG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Signal-Regulatory Protein Gamma (SIRPG) belongs to the signal-regulatory protein (SIRP) family whose members are receptor-type transmembrane glycoproteins which negatively regulate the receptor tyrosine kinase-coupled signaling processes. SIRPG is also a part of the immunoglobulin superfamily.

    • Synonyms

      signal-regulatory protein gamma isoform 1 precursor, bA77C3.1, CD172g, SIRP-B2, SIRPB2, SIRPgamma, Signal-Regulatory Protein Gamma, SIRPG, SIRP-b2, SIRP-beta-2, CD_antigen: CD172g, CD172 antigen-like family member B, Signal-regulatory protein beta-2, SIRP-gamma.

    • 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 MGSEEELQMI QPEKLLLVTV GKTATLHCTV TSLLPVGPVL WFRGVGPGRE LIYNQKEGHF PRVTTVSDLT KRNNMDFSIR ISSITPADVG TYYCVKFRKG SPENVEFKSG PGTEMALGAK PSAPVVLGPA ARTTPEHTVS FTCESHGFSP RDITLKWFKN GNELSDFQTN VDPTGQSVAY SIRSTARVVL DPWDVRSQVI CEVAHVTLQG DPLRGTANLS EAIRVPPTLE VTQQPMRVGN QVNVTCQVRK FYPQSLQLTW SENGNVCQRE TASTLTENKD GTYNWTSWFL VNISDQRDDV VLTCQVKHDG QLAVSKRLAL EVTVHQKDQS SDATP.

    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.

    Sirpg Human
  • View Data Sheet

    Name :

    EMG1 Human

    Description:

    EMG1 Nucleolar Protein Human Recombinant

    EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.

    Product # :

    PRO-1122

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    Description

    EMG1 Human Recombinant produced in E. coli is a single polypeptide chain containing 267 amino acids (1-244) and having a molecular mass of 29.1kDa.EMG1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The EMG1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM Nacl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    More Info

    • Introduction

      EMG1 is a 244 aa protein which has a role in ribosome biogenesis. EMG1 is a key protein in the small ribosomal subunit assembly, controls methylation during ribosome synthesis and takes part in pre-18S rRNA processing. EMG1 is localized to the nucleolus and a mutation in this gene is linked with Bowen-Conradi syndrome.

    • Synonyms

      EMG1 nucleolar protein homolog (S. cerevisiae), 18S rRNA Psi1248 methyltransferase, 18S rRNA (pseudouridine-N1-)-methyltransferase NEP1, Ribosome biogenesis protein NEP1, essential for mitotic growth 1, ribosomal RNA small subunit methyltransferase NEP1, Protein C2f, BWCNS, Grcc2f, NEP1, EC 2.1.1.-.

    • 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

      MGSSHHHHHH SSGLVPRGSH MGSMAAPSDG FKPRERSGGE QAQDWDALPP KRPRLGAGNK IGGRRLIVVL EGASLETVKV GKTYELLNCD KHKSILLKNG RDPGEARPDI THQSLLMLMD SPLNRAGLLQ VYIHTQKNVL IEVNPQTRIP RTFDRFCGLM VQLLHKLSVR AADGPQKLLK VIKNPVSDHF PVGCMKVGTS FSIPVVSDVR ELVPSSDPIV FVVGAFAHGK VSVEYTEKMV SISNYPLSAA LTCAKLTTAF EEVWGVI

    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.

    Emg1 Human
  • View Data Sheet

    Name :

    CASQ2 Dog

    Description:

    Calsequestrin-2 Dog

    Calsequestrin-2, Calsequestrin cardiac muscle isoform, CASQ2, CSQ.

    Product # :

    PRO-410

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    Description

    Calsequestrin is the major calcium storage protein of the sarcoplasmic reticulum. Intraluminar Ca2+ binds to calsequestrin during diastole to prevent Ca2+ precipitation and to lower its free ionic concentration to facilitate efficient storage. During systole, Calsequestrin coordinately releases ~40-­50 Ca2+ ions per molecule for each contraction-relaxation cycle by an uncertain mechanism. Calsequestrin has been shown to be of major importance in the regulation of cardiac excitation-contraction coupling.

    Source

    Dog Heart.

    Formulation

    The protein was lyophilized from a concentrated solution (1mg/ml) containing 10mM Tris-HCl and 1mM EGTA.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Synonyms

      Calsequestrin-2, Calsequestrin cardiac muscle isoform, CASQ2, CSQ.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized CASQ2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CASQ2 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 CASQ2 in sterile 18M-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.

    Casq2 Dog
  • View Data Sheet

    Name :

    ARL5A Human

    Description:

    ADP-Ribosylation Factor-Like 5A Human Recombinant

    ARL5, ARFLP5, ADP-ribosylation factor-like 5A.

    Product # :

    PRO-040

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    Description

    ARL5A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 203amino acids (1-179a.a.) and having a molecular mass of 23.3kDa.ARL5A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ARL5A protein solution (1mg/1ml) is formulated in 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.2mM PMSF and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      ARL5A is a member of the ARF family of GTP-binding proteins. ARFs are vital in eukaryotic vesicular trafficking pathways and have a crucial part in the activation of phospholipase D. Different from ARF family members, ARL5 is believed to lack ADP-ribosylation enhancing activity. ARL5A is developmentally regulated and has a role in nuclear dynamics and signaling cascades during embryonic development.

    • Synonyms

      ARL5, ARFLP5, ADP-ribosylation factor-like 5A.

    • 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 MGSHMGILFT RIWRLFNHQE HKVIIVGLDN AGKTTILYQF SMNEVVHTSP TIGSNVEEIV INNTRFLMWD IGGQESLRSS WNTYYTNTEF VIVVVDSTDR ERISVTREEL YKMLAHEDLR KAGLLIFANK QDVKECMTVA EISQFLKLTS IKDHQWHIQA CCALTGEGLC QGLEWMMSRL KIR

    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.

    Arl5A Human
  • View Data Sheet

    Name :

    b NGF Mouse

    Description:

    Beta-Nerve Growth Factor Mouse

    Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    Product # :

    CYT-440

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    Description

    NGF beta Mouse produced in Submaxillary Gland of Grown Mouse is a homodimer, non-glycosylated, polypeptide chain containing 2 identical 120 amino acids and having a molecular mass of 13,471 Dalton each.The NGF beta Mouse is purified by advanced biology purification technology.

    Source

    Submaxillary Gland of Grown Mouse.

    Formulation

    The NGF beta Mouse was lyophilized from solution containing 5% mannitol and 1% HSA.

    Purity

    Greater than 98% as determined by(a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE .

    Biological Activity

    The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

    More Info

    • Introduction

      NGF-beta has nerve growth stimulating activity and the complex is involved in the regulation of growth and the differentiation of sympathetic and certain sensory neurons. Mutations in this gene have been associated with hereditary sensory and autonomic neuropathy, type 5 (HSAN5), and dysregulation of this gene's expression is associated with allergic rhinitis.

    • Synonyms

      Beta Polypeptide, NGF, NGFB, HSAN5, Beta-NGF, MGC161426, MGC161428.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

    • Background

      What is the molecular weight/Mw of B NGF Protein?
      B NGF Protein has a total Mw of 13kDa.

      What is the source or expression system of B NGF Protein?
      Submaxillary Gland of Grown Mouse.

      What is the Purity of B NGF Protein?

      B NGF Protein is >98% pure as determined by SDS-PAGE.

      What is the Biological Activity of B NGF Protein?
      The method used to test the bioassay is the NGF-dependent survival of dorsal root ganglia neurons of chick embryo, corresponding to a Specific Activity of 500,000IU/mg.

      What is the amino acid sequence of B NGF Protein?
      SSTHPVFHMGEF SVCDSVSVWV GDKTTATDIK GKEVTVLAEV NINNSVFRQY FFETKCRASN PVESGCRGID SKHWNSYCTT THTFVKALTT DEKQAAWRFI RIDTACVCVL SRKATRRG.

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

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

    Beta Ngf Mouse
  • View Data Sheet

    Name :

    TRIM28 Human

    Description:

    Tripartite Motif Containing 28 Human Recombinant

    Transcription intermediary factor 1-beta, TIF1-beta, E3 SUMO-protein ligase TRIM28, KRAB-associated protein 1, KAP-1, KRAB-interacting protein 1, KRIP-1, Nuclear corepressor KAP-1, RING finger protein 96, Tripartite motif-containing protein 28, TRIM28, KAP1, RNF96, TIF1B, Tripartite motif containing 28, RNF96, TF1B.

    Product # :

    PRO-1697

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    Description

    TRIM28 Human Recombinant produced in E. coli is a single polypeptide chain containing 460 amino acids (366-802) and having a molecular mass of 48.7 kDa.TRIM28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TRIM28 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M Urea.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      Tripartite Motif Containing 28 (TRIM28) which is a member of the tripartite motif family includes 3 zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. TRIM28 mediates transcriptional control by interaction with the Kruppel-associated box repression domain found in many transcription factors. TRIM28 is restricted to the nucleus and connected with particular chromatin regions.

    • Synonyms

      Transcription intermediary factor 1-beta, TIF1-beta, E3 SUMO-protein ligase TRIM28, KRAB-associated protein 1, KAP-1, KRAB-interacting protein 1, KRIP-1, Nuclear corepressor KAP-1, RING finger protein 96, Tripartite motif-containing protein 28, TRIM28, KAP1, RNF96, TIF1B, Tripartite motif containing 28, RNF96, TF1B.

    • 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 MGSKLIYFQL HRALKMIVDP VEPHGEMKFQ WDLNAWTKSA EAFGKIVAER PGTNSTGPAP MAPPRAPGPL SKQGSGSSQP MEVQEGYGFG SGDDPYSSAE PHVSGVKRSR SGEGEVSGLM RKVPRVSLER LDLDLTADSQ PPVFKVFPGS TTEDYNLIVI ERGAAAAATG QPGTAPAGTP GAPPLAGMAI VKEEETEAAI GAPPTATEGP ETKPVLMALA EGPGAEGPRL ASPSGSTSSG LEVVAPEGTS APGGGPGTLD DSATICRVCQ KPGDLVMCNQ CEFCFHLDCH LPALQDVPGE EWSCSLCHVL PDLKEEDGSL SLDGADSTGV VAKLSPANQR KCERVLLALF CHEPCRPLHQ LATDSTFSLD QPGGTLDLTL IRARLQEKLS PPYSSPQEFA QDVGRMFKQF NKLTEDKADV QSIIGLQRFF ETRMNEAFGD.

    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.

    Trim28 Human
  • View Data Sheet

    Name :

    TGFB2 Human

    Description:

    Transforming Growth Factor Beta 2 Human Recombinant

    Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    Product # :

    CYT-441

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    Description

    TGFB2 Human Recombinant produced in plants is a homodimeric polypeptide chain containing 2 x 118 amino acids and having a total molecular mass of 27.08kDa. The TGFB2 is fused to 6xHis Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Nicotiana benthamiana.

    Formulation

    Lyophilized from a concentrated (1mg/ml) solution containing 50mM Tris-HCl pH-7.4.

    Purity

    Greater than 97.0% as determined by SDS-PAGE.

    Biological Activity

    The biological activity of TGFB2 is measured in culture by its ability to inhibit the mink lung epithelial (Mv1Lu) cells proliferation. ED50 < 40ng/ml, corresponding to a specific activity of 25,000 units/mg.

    More Info

    • Introduction

      TGFB2 is a 27.08 kDa protein having two identical 118 amino acid peptide chains linked by a single disulfide bond. TGFB2 is part of a family of five related cytokines that have an extensive variation of normal and neoplastic cells, indicating the importance of these homo-dimmer proteins as multi-functional regulators of cellular activity. The three mammalian isoforms of TGF-β (TGFb1, TGFb2 and TGFb3) signal through the same receptor and stimulate similar biological responses. They are involved in physiological processes as embryogenesis, tissue remodelling and wound healing.

    • Synonyms

      Transforming growth factor, beta 2, cetermin, Glioblastoma-derived T-cell suppressor factor, polyergin, G-TSF, TGF-beta2, TGF-beta-2, transforming growth factor beta-2, BSC-1 cell growth inhibitor, TGFB-2.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized TGFB2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TGFB2 Human 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 TGFB2 in sterile 18M-cm H2O not less than 1µg/40µl, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      HHHHHHALDAAYCFRNVQDNCCLRPLYIDFKRDLGWKWIH
      EPKGYNANFCAGACPYLWSSDTQHSRVLSLYNTINPEASAS
      PCCVSQDLEPLTI LYYIGKTPKIEQLSNMIVKSCKCS.

    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.

    Tgfb2 Human
  • View Data Sheet

    Name :

    TNNI1 Human Native

    Description:

    Troponin I Skeletal Muscle Human

    DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.

    Product # :

    PRO-2789

    Price :

    Quantity :

    Shipping Method :

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    Shipped at Room temp

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    More Info

    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    TNNI1 Native produced in Human skeletal is Immunological identity confirmed by reaction with monoclonal antibody that is specific for the Human Troponin I Skeletal Muscle. TNNI1 Native is purified by proprietary chromatographic technique.

    Source

    Human skeletal muscle.

    Formulation

    TNNI1 was lyophilized from 0.01M HCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Synonyms

      DKFZp451O223, SSTNI, TNN1, Troponin I, slow skeletal muscle, Troponin I, slow-twitch isoform.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Troponin I Skeletal Muscle although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution TNNI1 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 TNNI1 in Tris/urea buffer (20mM Tris, pH 7.5, 7M urea, 5mM EDTA, 15mM 2-mercaptoethanol) not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Background

      Troponin I, specifically the skeletal muscle isoform encoded by the TNNI1 gene, is a crucial regulator of muscle contraction. It functions as part of the troponin complex, which controls the interaction between actin and myosin filaments during muscle contraction. While extensive research has been conducted on troponin I in the context of cardiac muscle and cardiac diseases, the study of native human skeletal muscle troponin I remains an important but relatively understudied area. This research aims to provide a comprehensive exploration of native human skeletal muscle troponin I (TNNI1), elucidating its functions, structural significance, and potential applications in musculoskeletal research and clinical medicine.

      The primary objective of this research is to elucidate the physiological role of native human skeletal muscle TNNI1 in muscle contraction. Experiments involving human skeletal muscle tissue samples and isolated muscle fibers will be conducted to investigate how TNNI1 interacts with other components of the troponin complex and influences calcium-mediated muscle contraction. Understanding these mechanisms is fundamental for deciphering the complexities of skeletal muscle physiology and its implications for musculoskeletal health.

      The second objective is to assess the clinical relevance of native TNNI1 in muscle-related diseases. Clinical studies involving patients with various neuromuscular and muscle-wasting conditions will be conducted to evaluate the diagnostic and prognostic value of TNNI1 as a biomarker. These investigations may provide valuable insights into the use of native TNNI1 in the early detection and management of muscle disorders.

      The third objective is to explore the potential applications of native TNNI1 in musculoskeletal research and therapeutic development. Research will investigate the use of native TNNI1-expressing cells and tissues as models for studying muscle disorders and for developing novel therapeutic interventions targeting the troponin complex.

      By delving into the functions and roles of native human skeletal muscle TNNI1, this research aims to expand our knowledge of skeletal muscle physiology, its implications for muscle-related diseases, and its potential applications in musculoskeletal research and clinical medicine.

    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.

    Troponin 1 Skeletal Muscle
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