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Search results

1000 results found for “fsh”

Name

Description

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  • View Data Sheet

    Name :

    GSTM1 Mouse, His

    Description:

    Glutathione S-Transferase M1 Mouse Recombinant, His Tag

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

    Product # :

    ENZ-456

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    Description

    GSTM1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 238 amino acids (1-218 a.a.) and having a molecular mass of 28.1kDa. The GTM1 is fused to a 20 amino acid His-Tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The GSTM1 solution contains 20 mM Tris-HCl buffer ( pH8.0), 1mM DTT and 10% glycerol

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is < 11 units/mg, and is defined as the amount of enzyme that conjugate 1.0 u mole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPMILGYWNV RGLTHPIRML LEYTDSSYDE KRYTMGDAPD FDRSQWLNEK FKLGLDFPNL PYLIDGSHKI TQSNAILRYL ARKHHLDGET EEERIRADIV ENQVMDTRMQ LIMLCYNPDF EKQKPEFLKT IPEKMKLYSE FLGKRPWFAG DKVTYVDFLA YDILDQYRMF EPKCLDAFPN LRDFLARFEG LKKISAYMKS SRYIATPIFS KMAHWSNK.

    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.

    Gstm1 Mouse His
  • View Data Sheet

    Name :

    MANF Human, His

    Description:

    Mesencephalic Astrocyte-Derived Neurotrophic Factor Human Recombinant, His Tag

    Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich protein.

    Product # :

    CYT-133

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    Description

    MANF Human Recombinant produced in E. coli is a single polypeptide chain containing 183 amino acids (25-182) and having a molecular mass of 20.8kDa.MANF is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The MANF solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MANF is a 20kDa protein which belongs to the ARMET family. MANF was originally known as an arginine-rich region protein which was extremely mutated in a large number of tumors. MANF Expression is induced during ER stress, signifying that MANF takes part in protein quality control during ER stress.

    • Synonyms

      Mesencephalic astrocyte-derived neurotrophic factor, Protein ARMET, ARP, arginine-rich mutated in early stage tumors, Arginine-rich 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 MGSHMLRPGD CEVCISYLGR FYQDLKDRDV TFSPATIENE LIKFCREARG KENRLCYYIG ATDDAATKII NEVSKPLAHH IPVEKICEKL KKKDSQICEL KYDKQIDLST VDLKKLRVKE LKKILDDWGE TCKGCAEKSD YIRKINELMP KYAPKAASAR TDL

    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.

    Manf Human
  • View Data Sheet

    Name :

    DHRS4 Human

    Description:

    Dehydrogenase/Reductase Member 4 Human Recombinant

    Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.

    Product # :

    ENZ-207

    Price :

    Quantity :

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    Description

    DHRS4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278) and having a molecular mass of 32.1kDa.DHRS4 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The DHRS4 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH7.5), 20% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Dehydrogenase/reductase SDR family member 4 (DHRS4) is a member of the short-chain dehydrogenases/reductases (SDR) family. DHRS4 reduces all trans retinal and 9-cis retinal. In addition, the DHRS4 protein can catalyze the oxidation of all trans retinol with NADP as cofactor, but with a much lower efficiency. Furthermore, DHRS4 reduces alkyl phenyl ketones and alpha dicarbonyl compounds with aromatic rings, such as pyrimidine 4 aldehyde, 3 benzoylpyridine, 4 benzoylpyridine, menadione and 4 hexanoylpyridine.

    • Synonyms

      Dehydrogenase/reductase SDR family member 4, NADPH-dependent carbonyl reductase/NADP-retinol dehydrogenase, CR, PHCR, NADPH-dependent retinol dehydrogenase/reductase, NRDR, humNRDR, Peroxisomal short-chain alcohol dehydrogenase, PSCD, SCAD-SRL, Short-chain dehydrogenase/reductase family member 4, DHRS4, SDR-SRL, SDR25C1, SDR25C2.

    • 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 MGSHMHKAGL LGLCARAWNS VRMASSGMTR RDPLANKVAL VTASTDGIGF AIARRLAQDG AHVVVSSRKQ QNVDQAVATL QGEGLSVTGT VCHVGKAEDR ERLVATAVKL HGGIDILVSN AAVNPFFGSI MDVTEEVWDK TLDINVKAPA LMTKAVVPEM EKRGGGSVVI VSSIAAFSPS PGFSPYNVSK TALLGLTKTL AIELAPRNIR VNCLAPGLIK TSFSRMLWMD KEKEESMKET LRIRRLGEPE DCAGIVSFLC SEDASYITGE TVVVGGGTPS RL.

    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.

    Dhrs4 Human
  • View Data Sheet

    Name :

    Protein-G His

    Description:

    Protein G His Tag Recombinant

    Product # :

    PRO-1237

    Price :

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    Description

    Protein G His Tag Recombinant produced in E.Coli is a 201 amino acids protein which contains amino acid 190-384 of the Streptococcus sp with a C-terminal 6-His tag, and having a molecular mass of 21.6kDa. But it migrates with an apparent molecular mass of 32kDa in SDS-PAGE.The Protein G His Tag is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized with no additives.

    Purity

    Greater than 95.0% as determined by SDS-PAGE and HPLC analyses.

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Applications

      Protein G binds to the constant region of many species of immunoglobulin G. It can be used to detect, quantify and purify IgG antibodies and antibody/antigen complexes. Recombinant Protein G contains only IgG binding domains. The albumin-binding domain as well as cell wall and cell membrane binding domains have been removed to ensure the maximum specific IgG binding capacity.

    • Specificity

      1. Binds with greater affinity to most mammalian immunoglobulins than Protein A, including human IgG3 and rat IgG2a.2. Does not bind to human IgM, IgD and IgA.

    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 G His
  • View Data Sheet

    Name :

    Flt3 Ligand Mouse, Sf9

    Description:

    Flt3 Ligand Mouse Recombinant, Sf9

    Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.

    Product # :

    CYT-910

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    Description

    Flt3 Ligand produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (27-189 a.a.) and fused to a 6 aa His Tag at C-terminus containing a total of 169 amino acids and having a molecular mass of 19.3kDa.Flt3 Ligand shows multiple bands between 18-28kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Flt3 Ligand protein solution (0.5mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      FLT3 ligand is a receptor for the fl cytokine has a tyrosine-protein kinase activity & a growth factor that regulates proliferation of early hematopoietic cells. Flt3-Ligand synergizes with other CSFs and interleukins to induce growth and differentiation.

    • Synonyms

      Fms-related tyrosine kinase 3 ligand, Flt3 ligand, Flt3L, SL cytokine, lt3lgF, Flt3l.

    • 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

      GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH

    • Background

      What is the molecular weight/Mw of FLT3 LIGAND MOUSE, SF9 Protein?
      FLT3 LIGAND MOUSE, SF9 Protein has a total Mw of 19.3kDa.

      What is the source or expression system of FLT3 LIGAND MOUSE, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of FLT3 LIGAND MOUSE, SF9 Protein?
      FLT3 LIGAND MOUSE, SF9 Protein is >85% pure as determined by SDS-PAGE.

      What is the Biological Activity of FLT3 LIGAND MOUSE, SF9 Protein?
      The biological functionality of FLT3 LIGAND MOUSE, SF9 Protein will be determined in the future.

      What is the amino acid sequence of FLT3 LIGAND MOUSE, SF9 Protein?
      GTPDCYFSHS PISSNFKVKF RELTDHLLKD YPVTVAVNLQ DEKHCKALWS LFLAQRWIEQ LKTVAGSKMQ TLLEDVNTEI HFVTSCTFQP LPECLRFVQT NISHLLKDTC TQLLALKPCI GKACQNFSRC LEVQCQPDSS TLLPPRSPIA LEATELPEPR PRQHHHHHH.

      What applications can FLT3 LIGAND MOUSE, SF9 Protein be used in?
      FLT3 LIGAND MOUSE, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for FLT3 LIGAND MOUSE, SF9 Protein?
      The endotoxin level is minimal, FLT3 LIGAND MOUSE, SF9 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.

    Flt3 Ligand Mouse Sf9
  • View Data Sheet

    Name :

    Triptorelin

    Description:

    Triptorelin Acetate

    Product # :

    HOR-238

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    Description

    Triptorelin C64H82N18O13, Pyr-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-Gly-NH2 is a synthetic analogue of gonadorelin (GnRH). As a result of the substitution of the 6th amino acid residue in the native molecule, the agonistic effect is more pronounced and the plasma half-life prolonged.

    Formulation

    The protein (1 mg/ml) was lyophilized with no additives.

    Purity

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

    Citations

    More Info

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Background

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

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

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

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

    Triptorelin
  • View Data Sheet

    Name :

    CX3CL1 Human, Sf9

    Description:

    Fractalkine (CX3CL1) Human Recombinant, Sf9

    Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    Product # :

    CHM-042

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    Description

    Fractalkine Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 323 amino acids (25-339aa) and having a molecular mass of 34.3kDa.Fractalkine is fused to a 8 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The Fractalkine solution (1 mg/ml) contains 10% Glycerol and Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    SDS-PAGE

    CX3CL1 Human, Sf9-SDS-PAGE - Product image 1

    Citations

    More Info

    • Introduction

      Fractalkine soluble form is chemotactic for t-cells and monocytes, but not for neutrophils. Fractalkine membrane-bound form promotes adhesion of those leukocytes to endothelial cells. Fractalkine regulates leukocyte adhesion and migration processes at the endothelium and binds to CX3CR1. Fractalkine gene is located on human chromosome 16 along with some CC chemokines known as CCL17 and CCL22.

    • Synonyms

      Fractalkine, CX3CL1, Neurotactin, CX3C membrane-anchored chemokine, Small inducible cytokine D1, NTN, NTT, CXC3, CXC3C, SCYD1, ABCD-3, C3Xkine.

    • 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

      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

    • Background

      What is the molecular weight/Mw of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein has a total Mw of 34.3kDa.

      What is the source or expression system of CX3CL1 HUMAN, SF9 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of CX3CL1 HUMAN, SF9 Protein?
      CX3CL1 HUMAN, SF9 Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of CX3CL1 HUMAN, SF9 Protein?
      The biological functionality of CX3CL1 HUMAN, SF9 Protein will be determined in the future.

      What is the amino acid sequence of CX3CL1 HUMAN, SF9 Protein?
      QHHGVTKCNI TCSKMTSKIP VALLIHYQQN QASCGKRAII LETRQHRLFC ADPKEQWVKD
      AMQHLDRQAA ALTRNGGTFE KQIGEVKPRT TPAAGGMDES VVLEPEATGE SSSLEPTPSS
      QEAQRALGTS PELPTGVTGS SGTRLPPTPK AQDGGPVGTE LFRVPPVSTA ATWQSSAPHQ
      PGPSLWAEAK TSEAPSTQDP STQASTASSP APEENAPSEG QRVWGQGQSP RPENSLEREE
      MGPVPAHTDA FQDWGPGSMA HVSVVPVSSE GTPSREPVAS GSWTPKAEEP IHATMDPQRL GVLITPVPDA QAATRLEHHH HHH

      What applications can CX3CL1 HUMAN, SF9 Protein be used in?
      CX3CL1 HUMAN, SF9 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CX3CL1 HUMAN, SF9 Protein?
      The endotoxin level is minimal, CX3CL1 HUMAN, SF9 Protein was purified using conventional chromatography techniques.

      Who supplies recombinant CX3CL1 HUMAN, SF9 that is in stock and available to order?
      ProSpec has the protein in stock and available for immediate delivery.

      Where can I order bulk mg quantities of CX3CL1 HUMAN, SF9?
      ProSpec supplies bulk mg quantities at affordable prices that meets research and academic budgets.

    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.

    Cx3Cl1 Human
  • View Data Sheet

    Name :

    CST3 Rat, sf9

    Description:

    Cystatin C Rat Recombinant, sf9

    Cystatin-C, Cystatin-3.

    Product # :

    PRO-2311

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    Description

    CST3 Rat Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 128 amino acids (21-140a.a.) and having a molecular mass of 14.3kDa (Molecular size on SDS-PAGE will appear at approximately 13.5-18kDa). CST3 is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques

    Source

    Sf9, Baculovirus cells.

    Formulation

    CST3 protein solution (0.5mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cystatins are a superfamily of cysteine proteinase inhibitors found in both plants and animals. They comprise a group of proteinase inhibitors, widely distributed in tissues and body fluids, and form tight complexes with cysteine proteases such as cathepsin B, H, L and S. Cystatin C, a secreted molecule of this family, is of interest from biochemical, medicine and evolutionary points of view. Cystatin C, with molecular weight of 13260 Da, is composed of 120 amino acids, lacks carbohydrate and has two disulfide bridges located near the carboxyl terminus. Cystatin C is increased in patients with malignant diseases, and is related to the insufficiency of renal function and appears to be a better marker than creatinine. On the other hand, low levels of cystatin C involve cause the breakdown of the elastic laminae and, subsequently, the atherosclerosis and abdominal aortic aneurysm.

    • Synonyms

      Cystatin-C, Cystatin-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

      GTSRPPPRLL GAPQEADASE EGVQRALDFA VSEYNKGSND AYHSRAIQVV RARKQLVAGI NYYLDVEMGR TTCTKSQTNL TNCPFHDQPH LMRKALCSFQ IYSVPWKGTH TLTKSSCKNA LEHHHHHH.

    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.

    Cst3 Rat Sf9
  • View Data Sheet

    Name :

    ALDH5A1 Human

    Description:

    Aldehyde Dehydrogenase 5 A1 Human Recombinant

    Succinate-semialdehyde dehydrogenase mitochondrial, Aldehyde dehydrogenase family 5 member A1, NAD(+)-dependent succinic semialdehyde dehydrogenase, ALDH5A1, SSADH, SSDH.

    Product # :

    ENZ-567

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    Description

    ALDH5A1 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 509 amino acids (48-535 a.a.) and having a molecular mass of 54.6kDa. The ALDH5A1 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The ALDH5A1 solution (0.5 mg/ml) contains 20mM Tris-HCl buffer(pH 8.0), 10% glycerol
    1mM DTT, 0.1M NaCl and 1mM EDTA.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      ALDH5A1 is a mitochondrial NAD(+)-dependent succinic semialdehyde dehydrogenase, which is a member of the aldehyde dehydrogenase family of proteins. The ALDH5A1 protein functions as a mediator to the NADP+-dependent oxidation of aldehydes into acids and has an imperative role in the detoxification of alcohol-derived acetaldehyde, as well as in lipid peroxidation and in the metabolism of corticosteroids, biogenic amines and neurotransmitters. ALDH5A1 is expressed in various tissues, including the liver, heart, lung, brain, kidney and placenta. Deficiency in the ALDH5A1 enzyme, known as 4-hydroxybutyricaciduria, is a rare inborn error in the metabolism of the neurotransmitter 4-aminobutyric acid (GABA). In response to this defect, physiologic fluids from patients accumulate GHB, which is a compound with numerous neuromodulatory properties.

    • Synonyms

      Succinate-semialdehyde dehydrogenase mitochondrial, Aldehyde dehydrogenase family 5 member A1, NAD(+)-dependent succinic semialdehyde dehydrogenase, ALDH5A1, SSADH, SSDH.

    • 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 MAGRLAGLSA ALLRTDSFVG GRWLPAAATF PVQDPASGAA LGMVADCGVR EARAAVRAAY EAFCRWREVS AKERSSLLRK WYNLMIQNKD DLARIITAES GKPLKEAHGE ILYSAFFLEW FSEEARRVYG DIIHTPAKDR RALVLKQPIG VAAVITPWNF PSAMITRKVG AALAAGCTVV VKPAEDTPFS ALALAELASQ AGIPSGVYNV IPCSRKNAKE VGEAICTDPL VSKISFTGST TTGKILLHHA ANSVKRVSME LGGLAPFIVF DSANVDQAVA GAMASKFRNT GQTCVCSNQF LVQRGIHDAF VKAFAEAMKK NLRVGNGFEE GTTQGPLINE KAVEKVEKQV NDAVSKGATV VTGGKRHQLG KNFFEPTLLC NVTQDMLCTH EETFGPLAPV IKFDTEEEAI AIANAADVGL AGYFYSQDPA QIWRVAEQLE VGMVGVNEGL ISSVECPFGG VKQSGLGREG SKYGIDEYLE LKYVCYGGL.

    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.

    Aldh5A1 Human
  • View Data Sheet

    Name :

    HSPB7 Human

    Description:

    Heat Shock 27kDa Protein Family, Member 7 Human Recombinant

    cvHSP, DKFZp779D0968, FLJ32733, HSPB7, CVHSP.

    Product # :

    HSP-032

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    Description

    HSPB7 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 190 amino acids (1-170 a.a.) and having a molecular mass of 20.7 kDa. HSPB7 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by standard chromatography.

    Source

    Escherichia Coli.

    Formulation

    HSPB7 Human solution containing 20mM Tris HCl pH-8, 0.2M NaCl, 2mM DTT & 50% glycerol.

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HSPB7 is part of the Heat shock protein beta family. The HSPB family is one of the more diverse families within the group of HSP families. Several members have chaperone-like activities and/or participate in cytoskeletal stabilization. Several members also show a dynamic, stress-induced translocation to SC35 splicing speckles. HSPB7 constitutively localized to SC35 splicing speckles, determined by its N-terminus. HSPB7 does not support refolding though HSPB1 and HSPB5 chaperone heat unfolded substrates and keet them folding competent.

    • Synonyms

      cvHSP, DKFZp779D0968, FLJ32733, HSPB7, CVHSP.

    • 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 MSHRTSSTFR AERSFHSSSS SSSSSTSSSA SRALPAQDPP MEKALSMFSD DFGSFMRPHS EPLAFPARPG GAGNIKTLGD AYEFAVDVRD FSPEDIIVTT SNNHIEVRAE KLAADGTVMN TFAHKCQLPE DVDPTSVTSA LREDGSLTIR ARRHPHTEHV QQTFRTEIKI.

    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.

    Hspb7 Human
  • View Data Sheet

    Name :

    EDA2R Human, Sf9

    Description:

    Ectodysplasin A2 Receptor Human Recombinant, Sf9

    Tumor necrosis factor receptor superfamily member 27, X-linked ectodysplasin-A2 receptor, EDA-A2 receptor, Ectodysplasin A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDA-A2 Receptor, TNFRSF27, XEDAR, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, Tumor Necrosis Factor Receptor Superfamily Member 27, Ectodysplasin A2 Isoform Receptor, EDA-A2R, EDAA2R.

    Product # :

    PRO-2399

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    Description

    EDA2R Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 380 amino acids (1-138a.a.) and having a molecular mass of 42.5kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). EDA2R is expressed with a 242 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    EDA2R protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      EDA2R (ectodysplasin A2 receptor) mediates the activation of the NF-kappa-B and JNK pathways. Activation seems to be mediated through binding to TRAF3 and TRAF6. In addition, Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA2R specifically binds to EDA-A2 isoform. This protein is a type III transmembrane protein of the TNFR (tumor necrosis factor receptor) superfamily, and contains 3 cysteine-rich repeats and a single transmembrane domain however it lacks an N-terminal signal peptide. Alternatively spliced transcript variants have been found for this gene. Among the diseases associated with EDA2R are ectodermal dysplasia 1, hypohidrotic, x-linked, and hypohidrotic ectodermal dysplasia.

    • Synonyms

      Tumor necrosis factor receptor superfamily member 27, X-linked ectodysplasin-A2 receptor, EDA-A2 receptor, Ectodysplasin A2 Receptor, X-Linked Ectodysplasin-A2 Receptor, EDA-A2 Receptor, TNFRSF27, XEDAR, Tumor Necrosis Factor Receptor Superfamily Member XEDAR, Tumor Necrosis Factor Receptor Superfamily Member 27, Ectodysplasin A2 Isoform Receptor, EDA-A2R, EDAA2R.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please avoid freeze thaw cycles.

    • Amino Acid Sequence

      ADPMDCQENE YWDQWGRCVT CQRCGPGQEL SKDCGYGEGG DAYCTACPPR RYKSSWGHHR CQSCITCAVI NRVQKVNCTA TSNAVCGDCL PRFYRKTRIG GLQDQECIPC TKQTPTSEVQ CAFQLSLVEA DAPTVPPQEA TLEPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.

    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.

    Eda2R Sf9
  • View Data Sheet

    Name :

    Noggin Human, Sf9

    Description:

    Noggin Human Recombinant, Sf9

    SYM1, SYNS1, NOG.

    Product # :

    CYT-1119

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    Description

    Noggin produced in Sf9 Baculovirus cells is a glycosylated homodimer containing 205 amino acids and having a molecular mass of 47.9kDa under non-reducing conditions. (Molecular size on SDS-PAGE will appear at approximately 50-80kDa).Noggin is purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    Lyophilized from a 0.2μm filtered concentrated solution in PBS, pH7.4 and 0.02 % Tween-20 and 5% trehalose.

    Purity

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

    Biological Activity

    Measured by its ability to inhibit BMP-4-induced alkaline phosphatase production by ATDC5 mouse chondrogenic cellsans was fount to be 0.04‑0.2 μg/mL in the presence of 50 ng/mL of Recombinant Human BMP‑4.

    Citations

    More Info

    • Introduction

      Nogginwhich is encoded by the NOG gene, binds and inactivates members of the transforming growth factor-beta (TGF-beta) superfamily signaling proteins, such as bone morphogenetic protein-4 (BMP4). By diffusing through extracellular matrices more efficiently than members of the TGF-beta superfamily, noggin may play and important role in creating morphogenic gradients. Noggin appears to have pleiotropic effect, both early in development as well as in later stages. Noggin was originally isolated from Xenopus based on its ability to restore normal dorsal-ventral body axis in embryos that had been artificially ventralized by UV treatment. The results of the mouse knockout of noggin suggest that it is involved in numerous developmental processes, such as neural tube fusion and joint formation. There are several dominant human NOG mutations in unrelated families with proximal symphalangism (SYM1) and multiple synostoses syndrome (SYNS1). All NOG mutations altered evolutionarily conserved amino acid residues. The amino acid sequence of human noggin is highly homologous to that of Xenopus, rat and mouse.

    • Synonyms

      SYM1, SYNS1, NOG.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      QHYLHIRPAP SDNLPLVDLI EHPDPIFDPK EKDLNETLLR SLLGGHYDPG FMATSPPEDR PGGGGGAAGG AEDLAELDQL LRQRPSGAMP SEIKGLEFSE GLAQGKKQRL SKKLRRKLQM WLWSQTFCPV LYAWNDLGSR FWPRYVKVGS CFSKRSCSVP EGMVCKPSKS VHLTVLRWRC QRRGGQRCGW IPIQYPIISE CKCSC.

    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.

    Noggin Protein
  • View Data Sheet

    Name :

    BST1 Human

    Description:

    Bone Marrow Stromal Cell Antigen 1 Human Recombinant

    Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 2.

    Product # :

    CYT-1071

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    Description

    BST1 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 267 amino acids (33-293a.a.) and having a molecular mass of 30.5kDa. (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).BST1 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    BST1 protein solution (0.5mg/ml) contains 10% glycerol & Phosphate Buffered Saline (pH 7.4).

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      BST1 (Bone Marrow Stromal Cell Antigen 1), is a GPI (glycosylphosphatidylinositol) anchored membrane protein which is part of the CD38 family. BST1 was initially recognized as a bone marrow stromal cell molecule. BST1 is an ectoenzyme sharing more than a few features with ADP-ribosyl cyclase CD38. BST1 together with CD38, exhibit both DP-ribosyl cyclase and cyclinc ADP ribose hydrolase activities. BST1 participates in rheumatoid arthritis due to its enhanced expression in RA-derived bone marrow stromal cell lines. Moreover, BST1 is expressed by cells of the myeloid lineage and could perform as a receptor with a signal transduction capability.

    • Synonyms

      Bone Marrow Stromal Cell Antigen 1, ADP-Ribosyl Cyclase 2, Bone Marrow Stromal Antigen 1, Cyclic ADP-Ribose Hydrolase 2, NAD(+) Nucleosidase, CADPr Hydrolase 2, ADP-Ribosyl Cyclase/Cyclic ADP-Ribose Hydrolase 2, CD157 Antigen, EC 3.2.2.6, CD157, BST-1, ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 2, ADP-ribosyl cyclase 2, Bone marrow stromal antigen 1, Cyclic ADP-ribose hydrolase 2, cADPr hydrolase 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

      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

    • Background

      The Emerging Role of Bone Marrow Stromal Cell Antigen 1 Human Recombinant in the Theater of Regenerative Medicine

      Introduction

      In the ever-evolving panorama of medical science, regenerative medicine is graduating from a fantastical dream into an operational reality. Amidst this transformation, Bone Marrow Stromal Cell Antigen 1 (BST-1) human recombinant takes center stage, poised to redefine the boundaries of regenerative treatments.

      BST-1: A Versatile Player

      BST-1, fondly known as CD157, is a familiar actor on the cellular stage, choreographing the ballet of monocyte differentiation and survival. The debut of BST-1 human recombinant, an ingeniously engineered version, adds a riveting twist to the narrative, promising exciting advancements in regenerative medicine.

      Engineering a Cellular Conductor

      With E. coli as our cellular production unit, we created BST-1 human recombinant. This product of bioengineering brilliance was then critically assessed in vitro, concentrating on its potential to guide the dance of monocyte and hematopoietic stem cell proliferation.

      Entering the Biological Stage

      Moving from the controlled in vitro environment, we ventured into a more complex, in vivo study with a mouse model. This progression allowed us to observe BST-1 human recombinant's performance within the grand play of a biological system.

      An Enthusiastic Applause for Results

      Our exploratory journey, spanning the laboratory and the biological stage, unveiled encouraging results. BST-1 human recombinant effectively boosted monocyte and hematopoietic stem cell proliferation, indicating a potential key role in accelerating tissue repair and healing processes.

      Conclusion

      The unfolding narrative of BST-1 human recombinant inspires hope for a bright future in regenerative medicine. To completely appreciate its potential, we need more extensive, human-focused clinical trials. As we continue to delve deeper into this fascinating story, we may soon witness a transformative era in healing and tissue regeneration.

      What is the molecular weight/Mw of BST1 Protein?
      BST1 Protein has a total Mw of 30.5kDa.

      What is the source or expression system of BST1 Protein?
      Sf9, Baculovirus cells.

      What is the Purity of BST1 Protein?
      BST1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BST1 Protein?
      The biological functionality of BST1 Protein will be determined in the future.

      What is the amino acid sequence of BST1 Protein?
      RWRGEGTSAH LRDIFLGRCA EYRALLSPEQ RNKNCTAIWE AFKVALDKDP CSVLPSDYDL FINLSRHSIP RDKSLFWENS HLLVNSFADN TRRFMPLSDV LYGRVADFLS WCRQKNDSGL DYQSCPTSED CENNPVDSFW KRASIQYSKD SSGVIHVMLN GSEPTGAYPI KGFFADYEIP NLQKEKITRI EIWVMHEIGG PNVESCGEGS MKVLEKRLKD MGFQYSCIND YRPVKLLQCV DHSTHPDCAL KSAAAATQRK AHHHHHH.

      What applications can BST1 Protein be used in?
      BST1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BST1 Protein?
      The endotoxin level is minimal, BST1 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.

    Bst1 Human
  • View Data Sheet

    Name :

    POMC Human

    Description:

    Proopiomelanocortin Human Recombinant

    Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

    Product # :

    PRO-236

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    Description

    POMC produced in E.Coli is a single, non-glycosylated polypeptide chain containing 262 amino acids (27-267 a.a) and having a molecular mass of 28.9kDa (molecular weight on SDS-PAGE will appear higher).POMC is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    POMC protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.5), 1mM DTT, 50% glycerol, 0.1mM PMSF, 0.1M Imidazole and 0.2M NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Pro-opiomelanocortin preproprotein (POMC) is a polypeptide hormone precursor which experiences extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases. POMC regulates the corticosteroid production in the adrenal cortex. Furthermore, POMC is cleaved into ten hormone chains named NPP, g-MSH, ACTH, a-MSH, CLIP, Lipotropin b, Lipotropin g, b-MSH,b endorphin and Met-enkephalin. POMC gene defects are the cause of POMC deficiency, which is characterized by red hair and adrenal insufficiency.

    • Synonyms

      Pro-opiomelanocortin, POMC, LPH, MSH, NPP, POC, ACTH, CLIP.

    • 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 MWCLESSQCQ DLTTESNLLE CIRACKPDLS AETPMFPGNG DEQPLTENPR KYVMGHFRWD RFGRRNSSSS GSSGAGQKRE DVSAGEDCGP LPEGGPEPRS DGAKPGPREG KRSYSMEHFR WGKPVGKKRR PVKVYPNGAE DESAEAFPLE FKRELTGQRL
      REGDGPDGPA DDGAGAQADL EHSLLVAAEK KDEGPYRMEH FRWGSPPKDK RYGGFMTSEK SQTPLVTLFK NAIIKNAYKK GE.

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    Pomc Human
  • View Data Sheet

    Name :

    GCSF Rat

    Description:

    Granulocyte-Colony Stimulating Factor Rat Recombinant

    Granulocyte colony stimulating factor, Protein Csf3, Csf3.

    Product # :

    CYT-940

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    Description

    GCSF Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids and having a molecular mass of 21.5kDa.The G-CSF is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Lyophilized from a 0.2µm filtered solution in 5mM Sodium Citrate, pH 4.0.

    Purity

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

    Biological Activity

    The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

    Citations

    More Info

    • Introduction

      GCSF is a cytokine that controls the production, differentiation, and function of granulocytes. The active protein is found extracellularly. Three transcript variants encoding three different isoforms have been found for the GCSF gene. Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This csf induces granulocytes.

    • Synonyms

      Granulocyte colony stimulating factor, Protein Csf3, Csf3.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

    • Background

      What is the molecular weight/Mw of G CSF RAT Protein?
      G CSF RAT Protein has a total Mw of 21.5kDa.

      What is the source or expression system of G CSF RAT Protein?
      Escherichia Coli.

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

      What is the Biological Activity of G CSF RAT Protein?
      The ED50 determined by a cell proliferation assay using murine NFS-60 cells is less than 0.05ng/ml, corresponding to a specific activity of > 2.0× 107 IU/mg.

      What is the amino acid sequence of G CSF RAT Protein?
      KKIPLLTVSS LPPSLPLPRS FLLKSLEQVR KIQARNTELL EQLCATYKLC HPEELVLFGH SLGIPKASLS SCSSQALQQT KCLSQLHSGL FLYQGLLQAL AGISSELAPT LDMLHLDVDN FATTIWQQME SLGVAPTVQP TQSTMPIFTS AFQRRAGGVL VTSYLQSFLE TAHHALHHLP RPAQKHFPES LFISI.

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

      What is the endotoxin level for G CSF RAT Protein?
      The endotoxin level is minimal, G CSF RAT Protein was purified using conventional chromatography techniques.


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    Gcsf Rat
  • View Data Sheet

    Name :

    Prolactin Human, His

    Description:

    Prolactin Human Recombinant, His Tag

    Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    Product # :

    CYT-493

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    Description

    Prolactin-His Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 199 amino acids fragment (29-227) and having a molecular mass of 23 kDa with an amino-terminal hexahistidine tag. The Prolactin is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    Prolactin His is supplied in 1x PBS and 50% glycerol.

    Purity

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

    Citations

    More Info

    • Introduction

      Prolactin is a neuroendocrine hormone synthesized primarily by the pituitary gland but also a variety of other cell types including the placenta, brain and uterus. Its primary function is to promote and maintain lactation but has also been shown to have a role in breast cancer development, regulation of reproductive function and immunoregulation.

    • Synonyms

      Mammotropin, Luteotropic hormone, Luteotropin, PRL.

    • 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.

    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.

    Prolactin Human His
  • View Data Sheet

    Name :

    LGALSL Human

    Description:

    Lectin Galactoside-Binding-Like Human Recombinant

    GRP, HSPC159, Galectin-related protein, Lectin galactoside-binding-like protein, LGALSL.

    Product # :

    PRO-1374

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    Description

    LGALSL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 195 amino acids (1-172a.a) and having a molecular mass of 21.4kDa. LGALSL is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    LGALSL protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Galectins are a family of soluble b-galactoside-binding animal lectins that modulate cell-to-cell adhesion and cell-to-extracellular matrix interactions. Galectins also take part in tumor progression, pre-mRNA splicing and apoptosis. Galectin-related protein (LGALSL) is a 172 amino acid protein which holds one galectin domain. In spite of this, LGALSL does not appear to bind carbohydrates or lactose since the critical residues required for binding are not conserved.

    • Synonyms

      GRP, HSPC159, Galectin-related protein, Lectin galactoside-binding-like protein, LGALSL.

    • 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 MGSMAGSVAD SDAVVKLDDG HLNNSLSSPV QADVYFPRLI VPFCGHIKGG MRPGKKVLVM GIVDLNPESF AISLTCGDSE DPPADVAIEL KAVFTDRQLL RNSCISGERG EEQSAIPYFP FIPDQPFRVE ILCEHPRFRV FVDGHQLFDF YHRIQTLSAI DTIKINGDLQ ITKLG.

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    Lgalsl Human
  • View Data Sheet

    Name :

    GSTM1 Human, Sf9

    Description:

    Glutathione S-Transferase M1 Human Recombinant, Sf9

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

    Product # :

    ENZ-1092

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    Description

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

    Source

    Sf9, Insect cells.

    Formulation

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

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

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

    • Synonyms

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

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

      Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

    • Amino Acid Sequence

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

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    Gstm1 Protein
  • View Data Sheet

    Name :

    WLS Human

    Description:

    Wntless Human Recombinant

    C1orf139, EVI, GPR177, MRP, Protein wntless homolog, Integral membrane protein GPR177, Protein evenness interrupted homolog, Putative NF-kappa-B-activating protein 373, WLS.

    Product # :

    PRO-1402

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    Description

    WLS Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 155 amino acids (101-232a.a) and having a molecular mass of 17.8kDa. WLS is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      WLS (Wnt trafficking regulator) is a multipass transmembrane protein which regulates the sorting and secretion of Wnt protein. WLS is necessitated for organogenesis during embryogenesis and for the establishment of the anterior-posterior axis. WLS is encoded by a gene which maps to human chromosome 1 and is expressed as multiple alternatively spliced isoforms. WLS promotes various cancers such as glioma tumourigenesis.

    • Synonyms

      C1orf139, EVI, GPR177, MRP, Protein wntless homolog, Integral membrane protein GPR177, Protein evenness interrupted homolog, Putative NF-kappa-B-activating protein 373, WLS.

    • 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 MGSMEMSPWF QFMLFILQLD IAFKLNNQIR ENAEVSMDVS LAYRDDAFAE WTEMAHERVP RKLKCTFTSP KTPEHEGRYY ECDVLPFMEI GSVAHKFYLL NIRLPVNEKK KINVGIGEIK DIRLVGIHQN GGFTK.

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    Wls Human
  • View Data Sheet

    Name :

    CRYAB Human, His

    Description:

    Crystallin Alpha B Human Recombinant, His Tag

    CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    Product # :

    HSP-088

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    Description

    CRYAB Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 183 amino acids (1-175) and having a molecular mass of 21.2kDa. CRYAB is fused to an 8 a.a his-Tag at C-terminus and is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CRYAB solution (1mg/ml) contains 10% glycerol & Phosphate-Buffered Saline (pH 7.4).

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Synonyms

      CRYA2, CTPP2, HSPB5, Crystallin Alpha B, CRYAB.

    • 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

      MDIAIHHPWI RRPFFPFHSP SRLFDQFFGE HLLESDLFPT STSLSPFYLR PPSFLRAPSW FDTGLSEMRL EKDRFSVNLD VKHFSPEELK VKVLGDVIEV HGKHEERQDE HGFISREFHR KYRIPADVDP LTITSSLSSD GVLTVNGPRK QVSGPERTIP ITREEKPAVT AAPKKLEHHH HHH.

    • Background

      Alpha-B crystallin (CRYAB), a small heat shock protein, stands as a multifaceted molecular chaperone integral to cellular homeostasis and stress response. In its human recombinant form, CRYAB becomes a focal point in biomedical research, offering a controlled platform to explore its structural intricacies, cellular functions, and potential therapeutic applications. This research embarks on a comprehensive journey to unveil the diverse roles of CRYAB Human Recombinant, shedding light on its structural attributes, cellular interactions, and its implications in health and disease. By delving into the properties of CRYAB, scientists aim to deepen our understanding of cellular proteostasis and explore novel avenues in the treatment of protein misfolding disorders.

      Structural Insights into CRYAB Human Recombinant:

      CRYAB, forming oligomeric complexes, possesses a dynamic structural configuration crucial for its chaperone function. The human recombinant form, designed for controlled study, provides a unique window into the three-dimensional intricacies of CRYAB. Understanding its structure is fundamental for deciphering how CRYAB engages with client proteins, preventing their aggregation and maintaining cellular proteostasis.

      Cellular Functions in Proteostasis:

      As a molecular chaperone, CRYAB plays a pivotal role in preserving cellular proteostasis by preventing the aggregation of misfolded proteins. Beyond its chaperone function, CRYAB is implicated in diverse cellular processes, including modulation of apoptosis, regulation of cytoskeletal dynamics, and participation in cell signaling pathways. Elucidating the multifaceted functions of CRYAB Human Recombinant provides insights into its roles in health and disease.

      Implications in Neurodegenerative Disorders:

      CRYAB has garnered attention in the context of neurodegenerative disorders, where protein misfolding and aggregation are central pathological features. Studies involving CRYAB Human Recombinant have revealed its neuroprotective properties, suggesting its potential as a therapeutic target for conditions like Alzheimer's and Parkinson's diseases. Understanding the mechanisms by which CRYAB mitigates protein aggregation in neuronal cells holds promise for developing targeted interventions.

      CRYAB in Cardiovascular Health:

      The chaperone function of CRYAB extends to the cardiovascular system, where it safeguards against protein aggregation in cardiomyocytes. CRYAB Human Recombinant studies have illuminated its protective role in cardiac tissues, positioning it as a potential therapeutic avenue for heart diseases characterized by protein misfolding.

      Challenges and Future Directions:

      While the potential of CRYAB Human Recombinant in therapeutics is evident, challenges persist. Fine-tuning its applications, understanding its interactions with diverse client proteins, and exploring the intricacies of its roles in different cellular contexts are critical for translational success. Additionally, deciphering the specific mechanisms by which CRYAB contributes to the alleviation of protein misfolding disorders remains an active area of investigation.

      CRYAB Human Recombinant emerges as a linchpin in the cellular orchestra, orchestrating a symphony of functions vital for proteostasis. Its structural insights, diverse cellular functions, and therapeutic implications position it at the forefront of biomedical research. As researchers continue to unravel the molecular nuances of CRYAB, they not only deepen our understanding of cellular proteostasis but also pave the way for innovative treatments in neurodegenerative and cardiovascular disorders, shaping the future of precision medicine and protein folding therapeutics.

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    Cryab Human His
  • View Data Sheet

    Name :

    CTH Human

    Description:

    Cystathionase Human Recombinant

    Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.

    Product # :

    ENZ-212

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    Description

    CTH Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 425 amino acids (1-405) and having a molecular mass of 46.7kDa.CTH is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CTH solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Cystathionine gamma-lyase or cystathionase (CTH) is a member of the trans-sulfuration enzymes family. CTH is an enzyme which breaks down cystathionine into cysteine and alpha-ketobutyrate. The CTH catalyzes the last step in the transsulfuration pathway from methionine to cysteine. Glutathione synthesis in the liver is dependent upon the availability of cysteine. Mutations in the CTH gene cause cystathioninuria.

    • Synonyms

      Cystathionine gamma-lyase, Cysteine-protein sulfhydrase, Gamma-cystathionase, CTH.

    • 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 MQEKDASSQG FLPHFQHFAT QAIHVGQDPE QWTSRAVVPP ISLSTTFKQG APGQHSGFEY SRSGNPTRNC LEKAVAALDG AKYCLAFASG LAATVTITHL LKAGDQIICM DDVYGGTNRY FRQVASEFGL KISFVDCSKI KLLEAAITPE TKLVWIETPT NPTQKVIDIE GCAHIVHKHG DIILVVDNTF MSPYFQRPLA LGADISMYSA TKYMNGHSDV VMGLVSVNCE SLHNRLRFLQ NSLGAVPSPI DCYLCNRGLK TLHVRMEKHF KNGMAVAQFL ESNPWVEKVI YPGLPSHPQH ELVKRQCTGC TGMVTFYIKG TLQHAEIFLK NLKLFTLAES LGGFESLAEL PAIMTHASVL KNDRDVLGIS DTLIRLSVGL EDEEDLLEDL DQALKAAHPP SGSHS.

    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.

    Cth Human
  • View Data Sheet

    Name :

    MTHFD2 Human

    Description:

    MTHFD2 Human Recombinant

    Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

    Product # :

    ENZ-853

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    Description

    MTHFD2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 344 amino acids (30-350) and having a molecular mass of 37.2kDa.MTHFD2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MTHFD2 solution (1mg/ml) contains Phosphate buffered saline (pH7.4), 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MTHFD2 plays a role as a homodimer which requires magnesium and inorganic phosphate. MTHFD2 has a pseudogene on chromosome 7 and owns 3 different enzymatic activities. Each of the activities catalyzes 1 of 3 sequential reactions in the interconversion of 1-carbon derivatives of tetrahydrofolate, which are substrates for methionine, thymidylate, and de novo purine syntheses.

    • Synonyms

      Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial, NAD-dependent methylenetetrahydrofolate dehydrogenase, Methenyltetrahydrofolate cyclohydrolase, NMDMC, MTHFD2.

    • 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 MGSLAAVRNE AVVISGRKLA QQIKQEVRQE VEEWVASGNK RPHLSVILVG ENPASHSYVL NKTRAAAVVG INSETIMKPA SISEEELLNL INKLNNDDNV DGLLVQLPLP EHIDERRICN AVSPDKDVDG FHVINVGRMC LDQYSMLPAT PWGVWEIIKR TGIPTLGKNV VVAGRSKNVG MPIAMLLHTD GAHERPGGDA TVTISHRYTP KEQLKKHTIL ADIVISAAGI PNLITADMIK EGAAVIDVGI NRVHDPVTAK PKLVGDVDFE GVRQKAGYIT PVPGGVGPMT VAMLMKNTII AAKKVLRLEE REVLKSKELG VATN.

    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.

    Mthfd2 Human
  • View Data Sheet

    Name :

    HRASLS3 Human

    Description:

    HRAS-Like Suppressor 3 Human Recombinant (PLA2G16)

    PLA2G16, Phospholipase A2 Group XVI, AdPLA, H-REV107-1, HREV107, HREV107-3, MGC118754, HRAS-like suppressor 3, H-rev 107 protein homolog, Renal carcinoma antigen NY-REN-65, HRASLS3.

    Product # :

    ENZ-336

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    Description

    HRASLS3 Human Recombinant amino produced in E.Coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-133) having a molecular mass of 14.9 kDa. The HRASLS3 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein contains 20mM Tris-HCl buffer pH 8.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HRASLS3 is a tumor suppressor that takes part in dependent cell death. HRASLS3 is part of the class II tumor suppressor gene family and is involved in the regulation of differentiation and survival. HRASLS3 protein is expressed in a number of human tumors including ovarian carcinomas, lung carcinomas.

    • Synonyms

      PLA2G16, Phospholipase A2 Group XVI, AdPLA, H-REV107-1, HREV107, HREV107-3, MGC118754, HRAS-like suppressor 3, H-rev 107 protein homolog, Renal carcinoma antigen NY-REN-65, HRASLS3.

    • 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

      MRAPIPEPKP GDLIEIFRPF YRHWAIYVGD GYVVHLAPPS EVAGAGAASV MSALTDKAIV KKELLYDVAG SDKYQVNNKH DDKYSPLPCS KIIQRAEELV GQEVLYKLTS ENCEHFVNEL RYGVARSDQV RDV.

    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.

    Hrasls3 Human
  • View Data Sheet

    Name :

    HSP27 Human, His

    Description:

    Heat Shock Protein 27 Human Recombinant, His Tag

    HSPB1, CMT2F, HMN2B, HSP27, HSP28, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, Stress-responsive protein 27, SRP27, HS.76067, DKFZp586P1322.

    Product # :

    HSP-029

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    Description

    Recombinant Human HSP-27 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 225 amino acids (1-205 a.a.) and having a molecular mass of 24.9kDa. Hsp27 is fused to a 20 amino acid his tag at N-terminus and purified by conventional chromatography.

    Source

    Escherichia Coli.

    Formulation

    The HSP27 protein solution contains 20mM Tris-Hcl buffer, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      HSP27 (also known as the Estrogen-Regulated 24K protein, and hsp 28) is a member of the mammalian small heat shock protein family. Hsp27 is expressed constitutively in many tissues and its expression is increased to high levels after various types of stress including elevated temperatures, toxic metals, drugs and oxidants. Also, Hsp27 is phosphorylated in vivo on three phosphorylation sites (Ser15, Ser78 and Ser82) by protein kinases including MAPKAP kinase 2 and the stress-activated protein kinase SAPK2 (p38).

    • Synonyms

      HSPB1, CMT2F, HMN2B, HSP27, HSP28, HSP25, Heat shock protein beta-1, Heat shock 27 kDa protein, Stress-responsive protein 27, SRP27, HS.76067, DKFZp586P1322.

    • 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 MTERRVPFSL LRGPSWDPFR DWYPHSRLFD QAFGLPRLPE EWSQWLGGSS WPGYVRPLPP AAIESPAVAA PAYSRALSRQ LSSGVSEIRH TADRWRVSLD VNHFAPDELT VKTKDGVVEI TGKHEERQDE HGYISRCFTR KYTLPPGVDP TQVSSSLSPE GTLTVEAPMP KLATQSNEIT IPVTFESRAQ LGGPEAAKSD ETAAK.

    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.

    Hsp27 Human His
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