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Search results

653 results found for “biglycan”

Name

Description

Product #

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  • View Data Sheet

    Name :

    SNAPC1 Human

    Description:

    Small Nuclear RNA Activating Complex, Polypeptide 1 Human Recombinant

    PTFgamma, SNAP43, snRNA-activating protein complex subunit 1, SNAPc subunit 1, Proximal sequence element-binding transcription factor subunit gamma, PSE-binding factor subunit gamma, PTF subunit gamma, Small nuclear RNA-activating complex polypeptide 1, SNAPc 43 kDa subunit, SNAPC1.

    Product # :

    PRO-2085

    Price :

    Quantity :

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    • More Info

    Description

    SNAPC1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 391 amino acids (1-368 a.a) and having a molecular mass of 45.4kDa.SNAPC1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SNAPC1 protein solution (1mg/ml) contains 20mM Tris-HCl (pH 8.0) and 10% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Small Nuclear RNA Activating Complex, Polypeptide 1 (SNAPC1) is a part of the SNAPc complex necessary for the transcription of both RNA polymerase II and III small-nuclear RNA genes. SNAPC1 binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Moreover, SNAPC1 recruits TBP and BRF2 to the U6 snRNA TATA box.

    • Synonyms

      PTFgamma, SNAP43, snRNA-activating protein complex subunit 1, SNAPc subunit 1, Proximal sequence element-binding transcription factor subunit gamma, PSE-binding factor subunit gamma, PTF subunit gamma, Small nuclear RNA-activating complex polypeptide 1, SNAPc 43 kDa subunit, SNAPC1.

    • 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 MGSMGTPPGL QTDCEALLSR FQETDSVRFE DFTELWRNMK FGTIFCGRMR NLEKNMFTKE ALALAWRYFL PPYTFQIRVG ALYLLYGLYN TQLCQPKQKI RVALKDWDEV LKFQQDLVNA QHFDAAYIFR KLRLDRAFHF TAMPKLLSYR MKKKIHRAEV TEEFKDPSDR VMKLITSDVL EEMLNVHDHY QNMKHVISVD KSKPDKALSL IKDDFFDNIK NIVLEHQQWH KDRKNPSLKS KTNDGEEKME GNSQETERCE RAESLAKIKS KAFSVVIQAS KSRRHRQVKL DSSDSDSASG QGQVKATRKK EKKERLKPAG RKMSLRNKGN VQNIHKEDKP LSLSMPVITE EEENESLSGT EFTASKKRRK H.

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Snapc1 Human
  • View Data Sheet

    Name :

    Elcatonin

    Description:

    Elcatonin

    Product # :

    HOR-302

    Price :

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    Shipping Method :

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    • description
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    • biological activity
    • More Info

    Description

    Elcatonin Synthetic is a single, non-glycosylated polypeptide chain containing 31 amino acids, having a molecular mass of 3363.2 Dalton and a Molecular formula of C148H244N42O47.

    Formulation

    The protein was lyophilized with no additives.

    Purity

    Greater than 93.3% as determined by:
    (a) Analysis by RP-HPLC.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Biological Activity (based on net peptide) was found to be 6695.2 IU/mg.

    More Info

    • Introduction

      Elcatonin is a Calcitonin derivative which is transformed from eel´s calcitonin by changing the S-S bond into the stable C-N bond. It inhibits the absorption and autolysis of bones, thus leads to blood calcium descending. In addition, it inhibits the bone salts dissolving and transferring and promotes the excretion of calcium and phosphorus in urine. Meanwhile, it inhibits renal tubules reabsorbing calcium, phosphorus and sodium and keeps blood calcium at normal level. It is mainly used for remitting or eliminating the pain caused by Osteoporosis.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Amino Acid Sequence

      Ser-Asn-Leu-Ser-Thr-Asu-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Val-Gly-Ala-Gly-Thr-Pro-NH2.

    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.

    Elcatonin
  • View Data Sheet

    Name :

    SUMO1 Human His

    Description:

    Small Ubiquitin-Related Modifier 1 Human Recombinant, His Tag

    Small ubiquitin-related modifier 1, SUMO-1, Sentrin, Ubiquitin-like protein SMT3C, SMT3 homolog 3, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein UBL1, GAP-modifying protein 1, GMP1, SUMO1, SMT3C, SMT3H3, UBL1, PIC1, SMT3, DAP-1, OFC10, SENP2.

    Product # :

    PRO-980

    Price :

    Quantity :

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    • description
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    • More Info

    Description

    SUMO1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 109 amino acids (1-101) and having a molecular mass of 12.6 kDa.SUMO1 is fused to a 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SUMO1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 0.15M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    More Info

    • Introduction

      SUMO1 is a protein that belongs to the SUMO (small ubiquitin-like modifier) protein family. SUMO1 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. Still, unlike ubiquitin which targets proteins for degradation, SUMO1 is involved in a variety of cellular processes, for example nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO1 is not active until the last four amino acids of the carboxy-terminus are cleaved off.

    • Synonyms

      Small ubiquitin-related modifier 1, SUMO-1, Sentrin, Ubiquitin-like protein SMT3C, SMT3 homolog 3, Ubiquitin-homology domain protein PIC1, Ubiquitin-like protein UBL1, GAP-modifying protein 1, GMP1, SUMO1, SMT3C, SMT3H3, UBL1, PIC1, SMT3, DAP-1, OFC10, SENP2.

    • 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

      MSDQEAKPST EDLGDKKEGE YIKLKVIGQD SSEIHFKVKM TTHLKKLKES YCQRQGVPMN SLRFLFEGQR IADNHTPKEL GMEEEDVIEV YQEQTGGHST VLEHHHHHH

    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.

    Sumo1 Human His
  • View Data Sheet

    Name :

    BPIFA1 Human

    Description:

    BPI fold containing family A Member 1 Human Recombinant

    BPI fold-containing family A member 1, Lung-specific protein X, Nasopharyngeal carcinoma-related protein, Palate lung and nasal epithelium clone protein, Secretory protein in upper respiratory tracts, Tracheal epithelium-enriched protein, Von Ebner protein Hl, BPIFA1, LUNX, NASG, PLUNC, SPURT, SPLUNC1, bA49G10.5.

    Product # :

    PRO-404

    Price :

    Quantity :

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    • description
    • source
    • formulation
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    • More Info

    Description

    BPIFA1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 260 amino acids (20-256 a.a) and having a molecular mass of 27.1kDa.BPIFA1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    BPIFA1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 30% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BPI fold containing family A Member 1 (BPIFA1) belongs to the short subfamily of PLUNC family proteins and have homology only to the Nterminal domains of BPI. BPIFA1 is a secreted protein which is expressed in the secretory ducts and submucosal glands of tracheobronchial tissues. BPIFA1 binds to LPS (lipopolysaccharide) in nasal lavage fluid (NLF) which alludes to its role in the inflammatory response of the upper airways after exposure to irritants. BPIFA1 may also serve as a potential molecular marker for detection of micrometastasis in non-small-cell lung cancer. Decreased levels of BPIFA1 are observed in the NLF of smokers and people who have been exposed to reactive epoxy chemicals, which indicats that long-term exposure to airway irritants damages the production of BPIFA1 in the upper respiratory tract.

    • Synonyms

      BPI fold-containing family A member 1, Lung-specific protein X, Nasopharyngeal carcinoma-related protein, Palate lung and nasal epithelium clone protein, Secretory protein in upper respiratory tracts, Tracheal epithelium-enriched protein, Von Ebner protein Hl, BPIFA1, LUNX, NASG, PLUNC, SPURT, SPLUNC1, bA49G10.5.

    • 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 MGSQFGGLPV PLDQTLPLNV NPALPLSPTG LAGSLTNALS NGLLSGGLLG ILENLPLLDI LKPGGGTSGG LLGGLLGKVT SVIPGLNNII DIKVTDPQLL ELGLVQSPDG HRLYVTIPLG IKLQVNTPLV GASLLRLAVK LDITAEILAV RDKQERIHLV LGDCTHSPGS LQISLLDGLG PLPIQGLLDS LTGILNKVLP ELVQGNVCPL VNEVLRGLDI TLVHDIVNML IHGLQFVIKV.

    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.

    Bpifa1 Human
  • View Data Sheet

    Name :

    CAPNS1 Human

    Description:

    Calpain, Small Subunit 1 Human Recombinant

    Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    Product # :

    PRO-1965

    Price :

    Quantity :

    Shipping Method :

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    Description

    CAPNS1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 208 amino acids (84-268) and having a molecular mass of 23.8 kDa.CAPNS1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAPNS1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol and 1mM DTT.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Calpain, Small Subunit 1 (CAPNS1) belongs to the calpain small subunit family. Calpains are a ubiquitous, well-conserved family of calcium-dependent, cysteine proteases, widely distributed in mammalian cells. Calpain families are implicated in neurodegenerative processes, considering that their activation can be triggered by calcium influx and oxidative stress. Calpains function as heterodimers, comprising a specific large catalytic subunit (calpain 1 subunit in Calpain I, and calpain 2 subunit in Calpain II), and a common small regulatory subunit encoded by the CAPNS1 gene. The CAPNS1 protein is vital for the stability and function of both calpain heterodimers, whose proteolytic activities influence numerous cellular functions including apoptosis, proliferation, migration, adhesion, and autophagy.

    • Synonyms

      Calpain Small Subunit 1, CAPN4, Calcium-Activated Neutral Proteinase Small Subunit, Calcium-Dependent Protease Small Subunit 1, Calpain Regulatory Subunit, CANP Small Subunit, CDPS, CSS1, Calcium-Dependent Protease Small Subunit, Calcium-Dependent Protease Small Subunit, Calpain 4 Small Subunit (30K), Calpain Small Polypeptide, Calpain Small Subunit 1, CALPAIN4, CANPS, CAPNS, CANP, CAPNS1.

    • 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 MGSRTHYSNI EANESEEVRQ FRRLFAQLAG DDMEVSATEL MNILNKVVTR HPDLKTDGFG IDTCRSMVAV MDSDTTGKLG FEEFKYLWNN IKRWQAIYKQ FDTDRSGTIC SSELPGAFEA AGFHLNEHLY NMIIRRYSDE SGNMDFDNFI SCLVRLDAMF RAFKSLDKDG TGQIQVNIQE WLQLTMYS.

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    Capns1 Human
  • View Data Sheet

    Name :

    CAPS Human

    Description:

    Calcyphosine Human Recombinant

    Calcyphosin, Calcyphosine, CAPS, CAPS1, MGC126562.

    Product # :

    PRO-117

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    Description

    CAPS 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 209 amino acids (1-189 a.a.) and having a molecular mass of 23.1kDa. The CAPS is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CAPS solution (1 mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT and 100mM NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      Calcyphosine (CAPS) is a calcium-binding protein containing four EF-hand domains. CAPS protein was originally identified as thyroid protein p24 which is found in a number of epithelium and in some cells of the central nervous system. CAPS may have a role in the regulation of ion transport. In the thyroid follicular cells, CAPS is synthesized and phosphorylated in response to stimulation by thyrotropin and cAMP agonists.

    • Synonyms

      Calcyphosin, Calcyphosine, CAPS, CAPS1, MGC126562.

    • 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 MDAVDATMEK LRAQCLSRGA SGIQGLARFF RQLDRDGSRS LDADEFRQGL AKLGLVLDQA EAEGVCRKWD RNGSGTLDLE EFLRALRPPM SQAREAVIAA AFAKLDRSGD GVVTVDDLRG VYSGRAHPKV RSGEWTEDEV LRRFLDNFDS SEKDGQVTLA EFQDYYSGVS ASMNTDEEFV AMMTSAWQL.

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    Caps Human
  • View Data Sheet

    Name :

    UBE2D1 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D1 Human Recombinant

    Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.

    Product # :

    ENZ-116

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    Description

    UBE2D1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 170 amino acids (1-147 a.a.) and having a molecular mass of 19kDa.UBE2D1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2D1 solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 40% glycerol and 0.1M NaCl.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

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    • Introduction

      UBE2D1 is a member of the ubiquitin-conjugating enzyme family. Ubiquitination involves at least 3 classes of enzymes: ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s). UBE2D1 is strongly related to a stimulator of iron transport (SFT), and is up-regulated in hereditary hemochromatosis. In addition, UBE2D1 functions in the ubiquitination of the tumor-suppressor protein p53 and the hypoxia-inducible transcription factor HIF1alpha by interacting with the E1 ubiquitin-activating enzyme and the E3 ubiquitin-protein ligases.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 D1, Stimulator of Fe transport, SFT, UBC4/5 homolog, UbcH5, Ubiquitin carrier protein D1, Ubiquitin-conjugating enzyme E2(17)KB 1, Ubiquitin-conjugating enzyme E2-17 kDa 1, Ubiquitin-protein ligase D1, UBE2D1, SFT, UBC5A, UBCH5A, E2(17)KB1.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

      UBE2D1 Human Recombinant although stable at 4°C for 1 week, should be stored below -18°C. Please prevent freeze thaw cycles.

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMALKRIQ KELSDLQRDP PAHCSAGPVG DDLFHWQATI MGPPDSAYQG GVFFLTVHFP TDYPFKPPKI AFTTKIYHPN INSNGSICLD ILRSQWSPAL TVSKVLLSIC SLLCDPNPDD PLVPDIAQIY KSDKEKYNRH AREWTQKYAM.

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    Ube2D1 Human
  • View Data Sheet

    Name :

    UBE2D4 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D4 Human Recombinant

    Ubiquitin-conjugating enzyme E2D 4 (putative), UBCH5D, HBUCE1, Ubiquitin carrier protein D4, Ubiquitin-protein ligase D4, EC 6.3.2.19.

    Product # :

    ENZ-179

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    Description

    UBE2D4 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 167 amino acids (1-147) and having a molecular mass of 18.8 kDa.UBE2D4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      UBE2D4 is a member of the ubiquitin-conjugating enzyme family. Ubiquitin-conjugating enzymes (E2 enzymes or ubiquitin-carrier enzymes) execute the second step in the ubiquitination reaction which marks a protein for degradation using the proteasome. UBE2D4 receives ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro UBE2D4 can promote polyubiquitination using all 7 ubiquitin Lys residues, but usually selects 'Lys-11' and 'Lys-48'-linked polyubiquitination.

    • Synonyms

      Ubiquitin-conjugating enzyme E2D 4 (putative), UBCH5D, HBUCE1, Ubiquitin carrier protein D4, Ubiquitin-protein ligase D4, EC 6.3.2.19.

    • 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 MALKRIQKEL TDLQRDPPAQ CSAGPVGDDL FHWQATIMGP NDSPYQGGVF FLTIHFPTDY PFKPPKVAFT TKIYHPNINS NGSICLDILR SQWSPALTVS KVLLSICSLL CDPNPDDPLV PEIAHTYKAD REKYNRLARE WTQKYAM

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    Ube2D4 Human
  • View Data Sheet

    Name :

    UBE2T Human

    Description:

    Ubiquitin-Conjugating Enzyme E2T Human Recombinant

    EC 6.3.2.19, HSPC150, PIG50, Ubiquitin-conjugating enzyme E2 T, Ubiquitin-protein ligase T, Ubiquitin carrier protein T, Cell proliferation-inducing gene 50 protein, UBE2T.

    Product # :

    ENZ-506

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    Description

    UBE2T Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 205 amino acids (1-197 a.a.) and having a molecular mass of 23.6 kDa. The UBE2T is fused to an 8 amino acid His Tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2T solution contains 20mM Tris-HCl pH-8, 1mM DTT, and 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

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    • Introduction

      UBE2T is part of the E2 ubiquitin-conjugating enzyme family that participates in the protein degradation pathway. UBE2T catalyzes the ATP-dependent attachment of ubiquitin to target proteins, thus tagging them for subsequent destruction by the proteasome. UBE2T is an important factor of the Faconi anemia pathway of DNA damage repair and, upon self-inactivation, may negatively regulate the Faconi pathway.

    • Synonyms

      EC 6.3.2.19, HSPC150, PIG50, Ubiquitin-conjugating enzyme E2 T, Ubiquitin-protein ligase T, Ubiquitin carrier protein T, Cell proliferation-inducing gene 50 protein, UBE2T.

    • Physical Appearance

      Sterile Filtered clear 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

      MQRASRLKRE LHMLATEPPP GITCWQDKDQ MDDLRAQILG GANTPYEKGV FKLEVIIPER YPFEPPQIRF LTPIYHPNID SAGRICLDVL KLPPKGAWRP SLNIATVLTS IQLLMSEPNP DDPLMADISS EFKYNKPAFL KNARQWTEKH ARQKQKADEE EMLDNLPEAG DSRVHNSTQK RKASQLVGIE KKFHPDVLEH HHHHH.

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    Ube2T Human
  • View Data Sheet

    Name :

    CLNS1A Human

    Description:

    Chloride Channel, Nucleotide-Sensitive, 1A Human Recombinant

    CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.

    Product # :

    PRO-1277

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    Description

    CLNS1A Human Recombinant produced in E. coli is a single polypeptide chain containing 261 amino acids (1-237) and having a molecular mass of 28.8kDa (molecular size on SDS-PAGE will appear higher).CLNS1A is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CLNS1A solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 2mM DTT.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      Methylosome subunit pICln (CLNS1A), is a member of the pICln (TC 1.A.47) family. CLNS1A takes part in multiple regulatory pathways. CLNS1A interaction with Sm proteins, inhibits their compilation on U RNA and interferes with snRNP biogenesis. CLNS1A inhibits the binding of survival motor neuron protein (SMN) to Sm proteins. Methylosome subunit pICln is related with the plasma membrane where it functions as a chloride present regulator.

    • Synonyms

      CLNS1A, CLCI, ICLN, CLNS1B, Methylosome subunit pICln, Chloride channel, nucleotide sensitive 1A, Chloride conductance regulatory protein ICln, Chloride ion current inducer protein, Reticulocyte pICln.

    • 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 MGSHMSFLKS FPPPGPAEGL LRQQPDTEAV LNGKGLGTGT LYIAESRLSW LDGSGLGFSL EYPTISLHAL SRDRSDCLGE HLYVMVNAKF EEESKEPVAD EEEEDSDDDV EPITEFRFVP SDKSALEAMF TAMCECQALH PDPEDEDSDD YDGEEYDVEA HEQGQGDIPT FYTYEEGLSH LTAEGQATLE RLEGMLSQSV SSQYNMAGVR TEDSIRDYED GMEVDTTPTV AGQFEDADVD H.

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    Clns1A Human
  • View Data Sheet

    Name :

    RAB5C Human

    Description:

    RAB5C, Member RAS Oncogene Family Human Recombinant

    L1880, RAB5CL, RAB5L, RABL, Ras-related protein Rab-5C, RAB5C.

    Product # :

    PRO-1427

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    Description

    RAB5C Human Recombinant produced in E. coli is a single polypeptide chain containing 239 amino acids (1-216) and having a molecular mass of 25.9kDa. RAB5C is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The RAB5C solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

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    • Introduction

      RAB5C is a part of the Ras-related protein family. Members of the Rab protein family are small GTPases of the Ras superfamily guarantee reliability in the process of docking and fusion of vesicles with their right acceptor compartment.

    • Synonyms

      L1880, RAB5CL, RAB5L, RABL, Ras-related protein Rab-5C, RAB5C.

    • 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 MGSMAGRGGA ARPNGPAAGN KICQFKLVLL GESAVGKSSL VLRFVKGQFH EYQESTIGAA FLTQTVCLDD TTVKFEIWDT AGQERYHSLA PMYYRGAQAA IVVYDITNTD TFARAKNWVK ELQRQASPNI VIALAGNKAD LASKRAVEFQ EAQAYADDNS LLFMETSAKT AMNVNEIFMA IAKKLPKNEP QNATGAPGRN RGVDLQENNP ASRSQCCSN.

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    Rab5C Human
  • View Data Sheet

    Name :

    XRCC3 Human

    Description:

    X-Ray Repair Cross Complementing Protein 3 Human Recombinant

    X-ray repair cross complementing protein 3, RAD51-like.

    Product # :

    PRO-2649

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    Description

    XRCC3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 366 amino acids (1-346 a.a.) and having a molecular mass of 40 kDa. XRCC3 is fused to a 20 amino acid His tag at N-Terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The XRCC3 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 10% glycerol and 0.4M urea.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

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    • Introduction

      Recombinant Human X-Ray Repair Cross Complementing Protein 3, also referred to XRCC3, is a member of RecA family and RAD51 subfamily. The protein takes partin homologous recombination to maintain chromosome stability and repair DNA damage. XRCC3functionally complements Chinese hamster irs1SF, a repair-deficient mutant that shows hypersensitivity to a number of different DNA-damaging agents & chromosomally unstable.

    • Synonyms

      X-ray repair cross complementing protein 3, RAD51-like.

    • 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 MDLDLLDLNP RIIAAIKKAK LKSVKEVLHF SGPDLKRLTN LSSPEVWHLL RTASLHLRGS SILTALQLHQ QKERFPTQHQ RLSLGCPVLD ALLRGGLPLD GITELAGRSS AGKTQLALQL CLAVQFPRQH GGLEAGAVYI CTEDAFPHKR LQQLMAQQPR LRTDVPGELL QKLRFGSQIF IEHVADVDTL LECVNKKVPV LLSRGMARLV VIDSVAAPFR
      CEFDSQASAP RARHLQSLGA TLRELSSAFQ SPVLCINQVT EAMEEQGAAH GPLGFWDERV SPALGITWAN QLLVRLLADR LREEEAALGC PARTLRVLSA PHLPPSSCSY TISAEGVRGT PGTQSH

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    Xrcc3 Human
  • View Data Sheet

    Name :

    YWHAG Human

    Description:

    Tyr-3/Trp-5 Monooxygenase Activation Protein Gamma Human Recombinant

    14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    Product # :

    PKA-238

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    Description

    YWHAG Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 247 amino acids (1-247) and having a molecular mass of 28 kDa. YWHAG is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    YWHAG solution containing 20mM Tris 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      The 14-3-3 family of proteins plays a key regulatory role in signal transduction, checkpoint control, apoptotic and nutrient-sensing pathways. 14-3-3 proteins are highly conserved and ubiquitously expressed. There are at least seven isoforms that have been identified in mammals. The 14-3-3gamma, a subtype of the 14-3-3 family of proteins, was thought to be brain and neuron-specific. It has been shown to interact with RAF1 and protein kinase C, proteins involved in various signal transduction pathways.

    • Synonyms

      14-3-3 protein gamma, Protein kinase C inhibitor protein 1, KCIP-1, YWHAG, Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein, gamma polypeptide.

    • 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

      MVDREQLVQK ARLAEQAERY DDMAAAMKNV TELNEPLSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT SADGNEKKIE MVRAYREKIE KELEAVCQDV LSLLDNYLIK NCSETQYESK VFYLKMKGDY YRYLAEVATG EKRATVVESS EKAYSEAHEI SKEHMQPTHP IRLGLALNYS VFYYEIQNAP EQACHLAKTA FDDAIAELDT LNEDSYKDST LIMQLLRDNL TLWTSDQQDD DGGEGNN.

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    Ywhag Human
  • View Data Sheet

    Name :

    CYTL1 Human

    Description:

    Cytokine-Like 1 Human Recombinant

    Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

    Product # :

    CYT-775

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    Description

    CYTL1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (aa 23-136) containing 124 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 14.6kDa (calculated).

    Source

    Escherichia Coli.

    Formulation

    CYTL1 was filtered (0.4 µm) and lyophilized from 0.5mg/ml in 20mM Tris buffer and 50mM NaCl, pH 7.5.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Cytokine-like protein 1 (CYTL1) is a secreted protein. CYTL1 is expressed in CD34+ cell populations of bone marrow and cord blood which function as hematopoietic stem/progenitor cells. However, CYTL1 is not expressed in CD34- cells. Experiments with knock-out mice (Cytl1-/-) propose that CYTL1 is essential for the maintenance of cartilage homeostasis rather than cartilage and bone development, and loss of CYTL1 function is linked with experimental osteoarthritic cartilage destruction in mice.

    • Synonyms

      Cytokine-like protein 1, Protein C17, CYTL1, C4orf4, C17.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. CYTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

    • Background

      Title: Cytokine-Like 1 Human Recombinant: Exploring its Role in Immune Regulation and Therapeutic Potential

      Abstract:


      Cytokine-like 1 (CYTL1) is an emerging cytokine that exhibits pleiotropic effects on immune regulation and tissue homeostasis. This research paper provides a comprehensive analysis of human recombinant CYTL1, focusing on its production, characterization, and potential applications in immune modulation. The paper highlights the significance of CYTL1 in immune cell function, inflammation, and tissue repair. Furthermore, it explores ongoing research and clinical trials investigating the therapeutic potential of recombinant CYTL1 in various pathological conditions. The information presented in this paper aims to enhance our understanding of human recombinant CYTL1 and its utility as a research tool and a potential immunotherapeutic agent.

      Introduction:


      Cytokine-like 1 (CYTL1) is a recently discovered cytokine with diverse biological functions, including immune regulation and tissue repair. Human recombinant CYTL1, produced through genetic engineering techniques, provides researchers with a valuable tool to study its biological activities and explore its therapeutic potential.

      Production and Characterization:


      Recombinant CYTL1 is typically generated using expression systems such as mammalian cells or bacteria. The protein is then purified and characterized to ensure its structural integrity and functional activity. Rigorous quality control measures are implemented to confirm the specificity and bioactivity of the recombinant CYTL1.

      Role in Immune Regulation:


      CYTL1 has been shown to modulate immune cell function and inflammation. It can influence the differentiation and activation of various immune cell subsets, including T cells and macrophages. Recombinant CYTL1 serves as a valuable tool for investigating the mechanisms underlying immune regulation and exploring its potential as an immunomodulatory agent.

      Therapeutic Implications:


      The dysregulation of immune responses is associated with numerous pathological conditions, including autoimmune diseases and chronic inflammation. Recombinant CYTL1 holds promise as a potential immunotherapeutic agent due to its ability to modulate immune cell function and regulate inflammatory processes. Ongoing research and clinical trials are investigating the therapeutic applications of recombinant CYTL1 in various diseases, including autoimmune disorders and tissue regeneration.

      Conclusion:


      Human recombinant CYTL1 is a valuable research tool and a potential immunotherapeutic agent. Its production, characterization, and applications in immune regulation contribute to our understanding of immune responses and the development of targeted therapeutic interventions. Continued research and clinical trials exploring the therapeutic potential of recombinant CYTL1 offer promising avenues for improving outcomes in autoimmune diseases, chronic inflammation, and tissue repair.

      What is the molecular weight/Mw of CYTL1 Protein?
      CYTL1 Protein has a total Mw of 14.6kDa.

      What is the source or expression system of CYTL1 Protein?
      Escherichia Coli.

      What is the Purity of CYTL1 Protein?
      CYTL1 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of CYTL1 Protein?
      The biological functionality of CYTL1 Protein will be determined in the future.

      What is the amino acid sequence of CYTL1 Protein?
      MKHHHHHHASTPPTCYSRMR ALSQEITRDF NLLQVSEPSE PCVRYLPRLY LDIHNYCVLD KLRDFVASPP CWKVAQVDSL KDKARKLYTI MNSFCRRDLV FLLDDCNALE YPIPVTTVLP DRQR.

      What applications can CYTL1 Protein be used in?
      CYTL1 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for CYTL1 Protein?
      The endotoxin level is minimal, CYTL1 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.

    Cytl1 Human
  • View Data Sheet

    Name :

    LGALS4 Mouse

    Description:

    Galectin-4 Mouse Recombinant

    gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.

    Product # :

    CYT-187

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    • SDS-PAGE

    Description

    LGALS4 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 349 amino acids (1-326a.a) and having a molecular mass of 38.8kDa.LGALS4 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    LGALS4 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Biological Activity

    The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.

    SDS-PAGE

    LGALS4 Mouse-SDS-PAGE - Product image 1

    More Info

    • Introduction

      Galectin-4 is a member of the subfamily of galectins composed of two carbohydrate recognition domains having similar peptide chains. The galectins are a family of beta-galactoside-binding proteins having a role in modulating cell-cell and cell-matrix interactions, which inhibits chronic inflammations, GVHD, and allergic responses. LGALS4 expression is limited to small intestine, colon, and rectum, and it is underexpressed in colorectal cancer. LGALS4 binds as an endogenous ligand to glycosphingolipids having 3-O-sulfated Gal residues and bind as well to cholesterol-3-sulfate. LGALS4 takes part in cell adhesion. LGALS4 plays a role in crosslinking the lateral cell membranes of the surface-lining epithelial cells, thus supporting epithelial integrity against mechanical stress exerted by the bowel lume. LGALS4 is in charge of intestinal inflammation via selective regulation of peripheral and mucosal T-cell cell cycle, in addition to cell death by apoptosis of T-cells by a pathway independent of the activation of caspases. LGALS4 blockade decreases TNF-alpha inhibitor induced T-cell death. LGALS4 decreases pro-inflammatory cytokine secretion including IL-6 & IL-17.

    • Synonyms

      gal-4 , Galectin-4, Lactose-binding lectin 4, lectin galactoside-binding soluble 4.

    • 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 MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.

    • Background

      What is the molecular weight/Mw of LGALS4 MOUSE Protein?
      LGALS4 MOUSE Protein has a total Mw of 38.8kDa.

      What is the source or expression system of LGALS4 MOUSE Protein?
      Escherichia Coli.

      What is the Purity of LGALS4 MOUSE Protein?
      LGALS4 MOUSE Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of LGALS4 MOUSE Protein?
      The ED50 was measured by its ability to agglutinate human red blood cells and was found to be <5 ug/ml.

      What is the amino acid sequence of LGALS4 MOUSE Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMAYVPAP GYQPTYNPTL PYKRPIPGGL SVGMSVYIQG MAKENMRRFH VNFAVGQDDG ADVAFHFNPR FDGWDKVVFN TMQSGQWGKE EKKKSMPFQK GKHFELVFMV MPEHYKVVVN GNSFYEYGHR LPVQMVTHLQ VDGDLELQSI NFLGGQPAAA PYPGAMTIPA YPAGSPGYNP PQMNTLPVMT GPPVFNPRVP YVGALQGGLT VRRTIIIKGY VLPTARNFVI NFKVGSSGDI ALHLNPRIGD SVVRNSFMNG SWGAEERKVA YNPFGPGQFF DLSIRCGMDR FKVFANGQHL FDFSHRFQAF QMVDTLEING DITLSYVQI.

      What applications can LGALS4 MOUSE Protein be used in?
      LGALS4 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for LGALS4 MOUSE Protein?
      The endotoxin level is minimal, LGALS4 MOUSE Protein was purified using conventional chromatography techniques.


    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Lgals4 Mouse
  • View Data Sheet

    Name :

    BCL2 Human, His

    Description:

    B-Cell Lymphoma Protein 2 Alpha Human Recombinant, His Tag

    Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    Product # :

    PRO-683

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    Description

    BCL2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing amino acids 1-211 and having a molecular mass of 25.4 kDa. The BCL2 is fused to a 20 a.a. His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCL2 protein solution contains 20mM Tris-HCl, pH-8, 2mM DTT and 20% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BCL2 gene encodes an integral outer mitochondrial membrane protein that blocks the apoptotic death of some cells such as lymphocytes. Constitutive expression of BCL2, such as in the case of translocation of BCL2 to Ig heavy chain locus, is thought to be the cause of follicular lymphoma. Two transcript variants, produced by alternate splicing, differ in their C-terminal ends.

    • Synonyms

      Apoptosis regulator Bcl-2, BCL2, B-cell CLL/lymphoma 2, Bcl-2.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAHAGRTGYD NREIVMKYIH YKLSQRGYEW DAGDVGAAPP GAAPAPGIFS SQPGHTPHPA ASRDPVARTS PLQTPAAPGA AAGPALSPVP PVVHLTLRQA GDDFSRRYRR DFAEMSSQLH LTPFTARGRF ATVVEELFRD GVNWGRIVAF FEFGGVMCVE SVNREMSPLV DNIALWMTEY LNRHLHTWIQ DNGGWDAFVE LYGPSMRPLF D.

    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.

    Bcl2 Human His
  • View Data Sheet

    Name :

    BCL2L2 Human, His

    Description:

    BCL2 Like 2 Human Recombinant, His Tag

    B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.

    Product # :

    PRO-768

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    Description

    BCL2L2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 192 amino acids (1-172 a.a.) and having a molecular weight of 20.9kDa.The BCL2L2 is fused to a 20 a.a His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BCL2L2 protein solution contains 20mM Tris-HCl, pH-8, 100mM NaCl and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      BCL2L2 promotes cell survival and blocks dexamethasone-induced apoptosis. BCL2L2 mediates survival of postmitotic Sertoli cells by suppressing death-promoting activity of BAX. BCL2L2 is part of the BCL-2 protein family which form hetero- or homodimers and play an important role as anti and proapoptotic regulators. BCL2L2 causes reduced cell apoptosis under cytotoxic conditions. BCL2L2 is involved in the survival of NGF- and BDNF-dependent neurons. BCL2L2 plays an important role in adult spermatogenesis.

    • Synonyms

      B-Cell Lymphoma Protein 2, BCL2 Like 2, BCL2 Like protein 2, BCLW, Bcl2-L-2, Apoptosis regulator Bcl-W, BCL2L2, BCL-W, KIAA0271.

    • 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 MATPASAPDT RALVADFVGY KLRQKGYVCG AGPGEGPAAD PLHQAMRAAG DEFETRFRRT FSDLAAQLHV TPGSAQQRFT QVSDELFQGG PNWGRLVAFF VFGAALCAES VNKEMEPLVG QVQEWMVAYL ETRLADWIHS SGGWAEFTAL YGDGALEEAR RLREGNWASV RT.

    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.

    Bcl2L2 Human
  • View Data Sheet

    Name :

    BMP 5 Human

    Description:

    Bone Morphogenetic protein-5 Human Recombinant

    Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    Product # :

    CYT-660

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    • sds-page

    Description

    BMP-5 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 139 amino acids (317-454 a.a.) and having a total molecular mass of 15.7 kDa.BMP-5 is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The BMP-5 solution contains 10mM Sodium Citrate buffer (pH3.5) and 10% Glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    sds-page

    BMP5-sds-page - Product image 1

    More Info

    • Introduction

      BMP5 belongs to the bone morphogenetic protein family which is part of the transforming growth factor-beta superfamily. This superfamily is comprised of large families of growth and differentiation factors. Bone morphogenetic proteins were initially identified by their ability of demineralizing bone extract to induce endochondral osteogenesis in vivo in an extraskeletal site.
      BMP5 is an essential signaling molecule within the trabecular meshwork and optic nerve head, and may play a potential role in glaucoma pathogenesis. It was shown that BMP-5 increases the levels of osteopontin, BMP-2, alkaline phosphatase and core binding factor alpha 1 mRNAs in human periodontal (HPL) ligament cells. The BMP5 protein is expressed in normal synovial tissue and reduced in osteoarthritis and rheumatoid arthritis. BMP5 may have a role in certain cancers given that it is differentially regulated during the formation of different tumors.

    • Synonyms

      Bone morphogenetic protein 5, BMP-5, BMP5, MGC34244.

    • 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

      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

    • Background

      Bone Morphogenetic Protein-5 Human Recombinant: Unleashing the Potential for Tissue Engineering and Regenerative Medicine

      Abstract:

      Bone Morphogenetic Protein-5 (BMP-5) human recombinant is a pivotal member of the bone morphogenetic protein family, known for its crucial role in tissue development, repair, and regeneration. This research paper provides an in-depth analysis of BMP-5, including its characteristics, signaling pathways, and potential therapeutic applications. Additionally, innovative methodologies for the production and optimization of BMP-5 human recombinant are proposed, shedding light on its future implications in the field of tissue engineering and regenerative medicine.

      Introduction:

      Tissue engineering and regenerative medicine hold great promise for addressing the challenges of tissue repair and regeneration. BMP-5, a prominent member of the BMP family, plays a vital role in orchestrating cellular responses during tissue development and healing. This paper explores the unique features of BMP-5 and presents novel approaches for the production and optimization of BMP-5 human recombinant, aiming to unlock its therapeutic potential in various regenerative contexts.

      Characteristics and Signaling Pathways:

      BMP-5 is a secreted growth factor that belongs to the transforming growth factor-beta (TGF-β) superfamily. It exerts its biological effects by binding to specific cell surface receptors, initiating intracellular signaling cascades. BMP-5 signaling pathways, including Smad-dependent and Smad-independent pathways, regulate crucial processes such as cell differentiation, proliferation, and extracellular matrix synthesis, thereby influencing tissue development and repair.

      Production of BMP-5 Human Recombinant:

      Efficient production methodologies are crucial for harnessing the therapeutic potential of BMP-5 human recombinant. Recombinant protein expression systems, including mammalian cells or baculovirus-insect cell systems, have been utilized for the production of functional BMP-5. Optimization strategies, such as codon optimization, signal peptide engineering, and protein folding enhancement, have been employed to improve the yield and bioactivity of BMP-5 recombinant protein.

      Potential Therapeutic Applications:

      BMP-5 human recombinant holds tremendous potential in the field of tissue engineering and regenerative medicine. It plays a crucial role in bone formation, cartilage regeneration, and wound healing, making it a promising candidate for the treatment of skeletal disorders, osteochondral defects, and tissue injuries. Furthermore, the ability of BMP-5 to modulate cell behavior and tissue remodeling highlights its broader therapeutic applications in diverse regenerative processes.

      Conclusion:

      BMP-5 human recombinant emerges as a key regulator in tissue engineering and regenerative medicine, with significant implications for tissue repair and regeneration. Optimizing production methodologies and further elucidating its signaling mechanisms will enhance its therapeutic applications. With its involvement in bone and cartilage formation, as well as wound healing, BMP-5 human recombinant represents a promising tool for promoting tissue regeneration and addressing the challenges of tissue repair in various clinical contexts.

      What is the molecular weight/Mw of BMP5 Protein?
      BMP5 Protein has a total Mw of 15.7kDa.

      What is the source or expression system of BMP5 Protein?
      Escherichia Coli.

      What is the Purity of BMP5 Protein?
      BMP5 Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of BMP5 Protein?
      The biological functionality of BMP5 Protein will be determined in the future.

      What is the amino acid sequence of BMP5 Protein?
      MAANKRKNQN RNKSSSHQDS SRMSSVGDYN TSEQKQACKK HELYVSFRDL GWQDWIIAPE GYAAFYCDGE CSFPLNAHMN ATNHAIVQTL VHLMFPDHVP KPCCAPTKLN AISVLYFDDS SNVILKKYRN MVVRSCGCH.

      What applications can BMP5 Protein be used in?
      BMP5 Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for BMP5 Protein?
      The endotoxin level is minimal, BMP5 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.

    Bmp 5 Human
  • View Data Sheet

    Name :

    Leptin tA Ovine

    Description:

    Leptin Antagonist Triple Mutant Ovine Recombinant

    Product # :

    CYT-356

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    Description

    Leptin Antagonist Triple Mutant Ovine Recombinant is a single non-glycosilated polypeptide chain containing 146 amino and additional Ala at N-terminus acids and having a molecular mass of ~ 16 kDa, Leptin was mutated, resulting in L39A/D40A/F41A mutant. Leptin Antagonist Triple Mutant Ovine Recombinant was purified by proprietary chromatographic techniques.

    Source

    Escherichia coli.

    Formulation

    The protein was lyophilized from a concentrated (0.65mg/ml) solution with 0.003mM NaHCO3.

    Purity

    Greater than 98.0% as determined by:
    (a) Gel filtration analysis.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    ProSpec’s Leptin-Antagonist Triple Mutant Ovine Recombinant is capable of inhibiting leptin-induced proliferation of BAF/3 cells stably transfected with the long form of mouse leptin receptor. It also inhibits various leptin effects in several in vitro bioassays.

    More Info

    • Physical Appearance

      White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Leptin Antagonist Triple Mutant Ovine Recombinant although stable at room temperature for several weeks, should be stored desiccated below -18°C. Upon reconstitution at > 0.1 Lep-tA mutant mg/ml and up to 2 mM and filter sterilization Leptin mutant can be stored at 4°C or even room temperature for several weeks making it suitable for long term infusion studies using osmotic pumps. At lower concentration addition of a carrier protein (0.1% HSA or BSA) is suggested. Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized Leptin-Antagonist Triple Mutant Ovine Recombinant in sterile water or sterile 0.4% NaHCO3 adjusted to pH 8, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

    • Amino Acid Sequence

      The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Val-Pro-Ile-Arg.

    • Protein content

      Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.21 as the extinction coefficient for a 0.1% (1mg/ml) solution at pH 8.0. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics).

    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.

    Leptin Ta Ovine
  • View Data Sheet

    Name :

    UBE2I Human

    Description:

    Ubiquitin-Conjugating Enzyme E2I Human Recombinant

    SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    Product # :

    ENZ-341

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    Description

    UBE2I Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 158 amino acids (1-158 aa) & having a molecular mass of 18.0 kDa. UBE2I is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UBE2I (1mg/ml) contains 50mM HEPES (pH7.4) 150mM NaCl, 1mM DTT and 10% glycerol.

    Purity

    Greater than 95.0% as determined by Analysis by SDS-PAGE.

    More Info

    • Introduction

      Human Ubc9 is homologous to ubiquitin-conjugating enzymes (E2s). However, instead of conjugating ubiquitin, it conjugates a ubiquitin homologue, small ubiquitin-like modifier 1(SUMO-1). And hUbc9 retains striking structural and functional conservation with yeast Ubc9. The ubiquitin-dependent protein degradation system has been recognized as a complete enzymatic pathway that is responsible for the selective degradation of abnormal and short-lived proteins. The conjugation of ubiquitin requires the activities of ubiquitin-activating (E1) and –conjugating (E2) enzymes.

    • Synonyms

      SUMO-conjugating enzyme UBC9, EC 6.3.2.-, SUMO-protein ligase, Ubiquitin-conjugating enzyme E2 I, Ubiquitin-protein ligase I, Ubiquitin carrier protein I, Ubiquitin carrier protein 9, p18, UBC9, C358B7.1.

    • 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

      MSGIALSRLA QERKAWRKDH PFGFVAVPTK NPDGTMNLMN WECAIPGKKG TPWEGGLFKL RMLFKDDYPS SPPKCKFEPP LFHPNVYPSG TVCLSILEED KDWRPAITIK QILLGIQELL NEPNIQDPAQ AEAYTIYCQN RVEYEKRVRA QAKKFAPS.

    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.

    Ube2I Human
  • View Data Sheet

    Name :

    S100A8 Human, His

    Description:

    S100 Calcium Binding Protein A8 Human Recombinant, His Tag

    Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    Product # :

    PRO-150

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    Description

    The Recombinant Human S100A8 produced in E.coli has a molecular mass of 12.08kDa containing 103 amino acid residues of the human S100A8 and fused to a 10 a.a. His tag at N-terminus.

    Source

    Escherichia Coli.

    Formulation

    S100A8 was filtered (0.4µm) and lyophilized in 0.5mg/ml in 20mM Tris and 100mM NaCl, pH 7.5.

    More Info

    • Introduction

      S100A8 is a part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a broad range of cells, and participate in the regulation of cellular processes such as cell cycle progression and differentiation. S100A8 plays a role in the inhibition of casein kinase and as a cytokine. S100A8 altered expression is related with cystic fibrosis disease. S100A8 is a calcium-binding protein that has antimicrobial activity against bacteria and fungi.S100A8 is crucial for resistance towards invasion by pathogenic bacteria. S100A8 up-regulates transcription of genes that are under the control of NF-kappa-B. S100A8 plays a role in the development of endotoxic shock in response to bacterial lipopolysaccharide. S100A8 endorses tubulin polymerization and promotes phagocyte migration and infiltration of granulocytes at sites of wounding. S100A8 takes part as a pro-inflammatory mediator in acute and chronic inflammation and up-regulates the release of IL8 and cell-surface expression of ICAM1.

    • Synonyms

      Calgranulin A, MRP8, CAGA, CGLA, CFAG, Protein S100-A8, S100 calcium-binding protein A8, Migration inhibitory factor-related protein 8, MRP-8, p8, Cystic fibrosis antigen, Leukocyte L1 complex light chain, Calprotectin L1L subunit, Urinary stone protein band A, S100A8, MIF, NIF, L1Ag, CP-10, MA387, 60B8AG.

    • Stability

      Store lyophilized protein at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles. Reconstituted protein can be stored at 4°C for a limited period of time; it does not show any change after two weeks at 4°C.

    • Solubility

      It is recommended to add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

    • Amino Acid Sequence

      MKHHHHHHAS MLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQEMLTELEKALN SIIDVYHKYS LIKGNFHAVY RDDLKKLLET ECPQYIRKKG ADVWFKELDI NTDGAVNFQE FLILVIKMGV AAHKKSHEES HKE.

    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.

    S100A8 Human His
  • View Data Sheet

    Name :

    MYLPF Human

    Description:

    Myosin Light chain, Phosphorylatable, Fast Skeletal Muscle Human Recombinant

    Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    Product # :

    PRO-243

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    Description

    MYLPF produced in E.Coli is a single, non-glycosylated polypeptide chain containing 189 amino acids (1-169 a.a) and having a molecular mass of 21.2kDa.MYLPF is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    MYLPF protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 100mM NaCl.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Myosin regulatory light chains, including MRCL3, MYLPF and MYL9, regulate contraction in smooth muscle and non-muscle cells via phosphorylation by MLCK (myosin light chain kinase). Phosphorylation of myosin regulatory light chains, catalyzed by MLCK in the presence of calcium and calmodulin, increases the actin-activated myosin ATPase activity, thus regulating the contractile activity. MYLPF is vital for fast and slow skeletal muscle development.

    • Synonyms

      Myosin regulatory light chain 2 skeletal muscle isoform, Fast skeletal myosin light chain 2, MLC2B, MYLPF, MRLC2, MYL11, HUMMLC2B.

    • 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 MAPKRAKRRT VEGGSSSVFS MFDQTQIQEF KEAFTVIDQN RDGIIDKEDL RDTFAAMGRL NVKNEELDAM MKEASGPINF TVFLTMFGEK LKGADPEDVI TGAFKVLDPE GKGTIKKKFL EELLTTQCDR FSQEEIKNMW AAFPPDVGGN VDYKNICYVI THGDAKDQE.

    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.

    Mylpf Human
  • View Data Sheet

    Name :

    NECTIN1 Human

    Description:

    Nectin Cell Adhesion Molecule 1 Human Recombinant

    PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    Product # :

    PRO-2648

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    • description
    • source
    • formulation
    • purity
    • More Info

    Description

    NECTIN1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 334amino acids (31-355a.a) and having a molecular mass of 37.3kDa.NECTIN1 is fused to an 9 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

    The NECTIN1 solution (1mg/ml) contains Phosphate-Buffered Saline (pH 7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      Nectin-1, also referred to as ED4, is a poliovirus receptor- related 1 protein is a part of the Nectin family. Nectin-1 endorses cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions among PVRL1/nectin-1 & PVRL4/nectin-4 and among PVRL1/nectin-1 & PVRL3/nectin-3 have been found. Nectin-1 acts as an entry receptor for herpes simplex virus & pseudorabies virus as well. Likewise, Neurite outgrowth-promoting activity has been shown by Nectin-1.

    • Synonyms

      PVRL1, CD111, CLPED1, ED4, HIgR, HVIS, HVEC, Nectin-1, OFC7, PRR, PRR1, PVRR, PVRR1, SK-12.

    • 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

      ADPQVVQVND SMYGFIGTDV VLHCSFANPL PSVKITQVTW QKSTNGSKQN VAIYNPSMGV SVLAPYRERV EFLRPSFTDG TIRLSRLELE DEGVYICEFA TFPTGNRESQ LNLTVMAKPT NWIEGTQAVL RAKKGQDDKV LVATCTSANG KPPSVVSWET RLKGEAEYQE IRNPNGTVTV ISRYRLVPSR EAHQQSLACI VNYHMDRFKE SLTLNVQYEP EVTIEGFDGN WYLQRMDVKL
      TCKADANPPA TEYHWTTLNG SLPKGVEAQN RTLFFKGPIN YSLAGTYICE ATNPIGTRSG QVEVNITEFP YTPSPPEHGR RAGPVPTAHH HHHH

    ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

    Nectin1 Human
  • View Data Sheet

    Name :

    ARMC10 Human

    Description:

    Armadillo Repeat Containing 10 Human Recombinant

    Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    Product # :

    PRO-1453

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    Description

    ARMC10 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 304 amino acids (28-308 a.a) and having a molecular mass of 33.6 kDa.ARMC10 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    ARMC10 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.

    Purity

    Greater than 85.0% as determined by SDS-PAGE.

    More Info

    • Introduction

      AMRC10 is a protein which contains an armadillo repeat and transmembrane domain. Upregulation of the AMRC10 gene has a role in hepatocellular carcinoma. AMRC10 decreases the transcriptional activity of the tumor suppressor protein p53 through direct interaction with the DNA-binding domain of p53, moreover it might play a role in cell growth and survival.

    • Synonyms

      Armadillo repeat-containing protein 10, Splicing variant involved in hepatocarcinogenesis protein, ARMC10, SVH.

    • 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 MGSTRGRRRG DRELGIRSSK SAEDLTDGSY DDVLNAEQLQ KLLYLLESTE DPVIIERALI TLGNNAAFSV NQAIIRELGG IPIVANKINH SNQSIKEKAL NALNNLSVNV ENQIKIKIYI SQVCEDVFSG PLNSAVQLAG LTLLTNMTVT NDHQHMLHSY ITDLFQVLLT GNGNTKVQVL KLLLNLSENP AMTEGLLRAQ VDSSFLSLYD SHVAKEILLR VLTLFQNIKN CLKIEGHLAV QPTFTEGSLF FLLHGEECAQ KIRALVDHHD AEVKEKVVTI IPKI.

    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.

    Armc10 Human
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