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1000 results found for “MANF”
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Name :
NCALD HumanDescription:
Neurocalcin Delta Recombinant Human
Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.
Product # :
PRO-093Price :
Quantity :
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Shipped with Ice Packs
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Description
NCALD produced in E.Coli is a single, non-glycosylated polypeptide chain containing 213 amino acids (1-193.a.a) and having a molecular mass of 24.4kDa. NCALD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NCALD protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 100mM NaCl, 1mM DTT and 40% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
NCALD belongs to the neuronal calcium sensor (NCS) family. NCALD is cytosolic at inactive calcium levels; but, high intracellular calcium levels induce a conformational transformation which exposes the myristoyl group, causing protein association with membranes and partial co-localization with the perinuclear trans-golgi network. NCALD protein is a regulator of signal transduction by G protein-coupled receptor.
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Synonyms
Rocalcin Delta, MGC33870, MGC74858, Neurocalcin-Delta.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGKQNSKLRP EVMQDLLEST DFTEHEIQEW YKGFLRDCPS GHLSMEEFKK IYGNFFPYGD ASKFAEHVFR TFDANGDGTI DFREFIIALS VTSRGKLEQK LKWAFSMYDL DGNGYISKAE MLEIVQAIYK MVSSVMKMPE DESTPEKRTE KIFRQMDTNR DGKLSLEEFI RGAKSDPSIV RLLQCDPSSA GQF.
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.
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Name :
EEF1E1 HumanDescription:
Eukaryotic Translation Elongation Factor 1 Epsilon 1 Human Recombinant
Eukaryotic translation elongation factor 1 epsilon-1, Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3, Elongation factor p18, Multisynthase complex auxiliary component p18, EEF1E1, AIMP3, P18.
Product # :
PRO-199Price :
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Shipped with Ice Packs
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Description
EEF1E1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 194 amino acids (1-174 a.a.) and having a molecular mass of 21.9kDa.EEF1E1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EEF1E1 solution (1mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 20% glycerol 0.1M NaCl and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1) shares sequence similarity with the amino-terminal ends of the Beta and Gamma subunits of EF-1. By specifically interacting with MetRS, EEF1E1 binds to a macromolecular tRNA synthtase complex which catalyzes the ligation of specific amino acids to their cognate tRNAs. Upon DNA damage, EEF1E1 translocates to the nucleus where it interacts with ATM and ATR, resulting in p53 activation.
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Synonyms
Eukaryotic translation elongation factor 1 epsilon-1, Aminoacyl tRNA synthetase complex-interacting multifunctional protein 3, Elongation factor p18, Multisynthase complex auxiliary component p18, EEF1E1, AIMP3, P18.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAAAAELSLL EKSLGLSKGN KYSAQGERQI PVLQTNNGPS LTGLTTIAAH LVKQANKEYL LGSTAEEKAI VQQWLEYRVT QVDGHSSKND IHTLLKDLNS YLEDKVYLTG YNFTLADILL YYGLHRFIVD LTVQEKEKYL NVSRWFCHIQ HYPGIRQHLS SVVFIKNRLY TNSH.
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.
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Name :
EIF5A HumanDescription:
Eukaryotic Translation Initiation Factor 5A Human Recombinant
EIF-5A, EIF5A1, eIF5AI, MGC99547, MGC104255, EIF5A, Eukaryotic translation initiation factor 5A-1, eIF-5A-1, eIF-5A1, Eukaryotic initiation factor 5A isoform 1, eIF-4D, Rev-binding factor.
Product # :
PRO-674Price :
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Shipped with Ice Packs
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Description
EIF5A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 154 amino acids and having a molecular mass of 16.8 kDa. EIF5A is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The EIF5A protein solution (1mg/ml) contains 50mM Tris-HCl, pH-7.5 and 10% Glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
EIF5A is the single protein identified to contain remarkable amino acid formed by the action of deoxyhypusine synthase and deoxyhypusine hydroxylase using spermidine as the substrate. EIF5A takes part in the first step of peptide bond formation in translation, nevertheless further experiments implicates it as a universally conserved translation elongation factor. Modulation of EIF5A is connected to proliferation and cancer. Expression of EIF-5A is upregulated in the PBMCs of HIV-1 patients. EIF5A coordinates significant cellular processes like cell viability and senescence during its effects on the stability of certain mRNAs. Heat stress-induced loss of EIF-5A in a human pancreatic cancer cell line. EIF5A stability takes part in determining the fate of the particular cell type after severe heat stress.
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Synonyms
EIF-5A, EIF5A1, eIF5AI, MGC99547, MGC104255, EIF5A, Eukaryotic translation initiation factor 5A-1, eIF-5A-1, eIF-5A1, Eukaryotic initiation factor 5A isoform 1, eIF-4D, Rev-binding factor.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MADDLDFETG DAGASATFPM QCSALRKNGF VVLKGRPCKI VEMSTSKTGK HGHAKVHLVG IDIFTGKKYE DICPSTHNMD VPNIKRNDFQ LIGIQDGYLS LLQDSGEVRE DLRLPEGDLG KEIEQKYDCG EEILITVLSA MTEEAAVAIK AMAK.
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.
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Name :
LANCL1 HumanDescription:
LanC Lantibiotic Synthetase Component C-Like 1 Human Recombinant
GPR69A, p40, LanC-like protein 1, 40 kDa erythrocyte membrane protein, LANCL1.
Product # :
PRO-2004Price :
Quantity :
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Shipped with Ice Packs
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Description
LANCL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 422 amino acids (1-399a.a) and having a molecular mass of 47.7kDa. LANCL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LANCL1 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.15M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
LanC Lantibiotic Synthetase Component C-Like 1 (LANCL1) belongs to the LanC family although formerly considered a part of the G-proteincoupled receptor superfamily. LANCL1 takes part in the biosynthesis of antimicrobial peptides. LANCL1 functions as a peptide-modifying enzyme component in eukaryotic cells. LANCL1 participates in EPS8 signaling and binds glutathione.
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Synonyms
GPR69A, p40, LanC-like protein 1, 40 kDa erythrocyte membrane protein, LANCL1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAQRAFP NPYADYNKSL AEGYFDAAGR LTPEFSQRLT NKIRELLQQM ERGLKSADPR DGTGYTGWAG IAVLYLHLYD VFGDPAYLQL AHGYVKQSLN CLTKRSITFL CGDAGPLAVA AVLYHKMNNE KQAEDCITRL IHLNKIDPHA PNEMLYGRIG YIYALLFVNK NFGVEKIPQS HIQQICETIL TSGENLARKR NFTAKSPLMY EWYQEYYVGA AHGLAGIYYY LMQPSLQVSQ GKLHSLVKPS VDYVCQLKFP SGNYPPCIGD NRDLLVHWCH GAPGVIYMLI QAYKVFREEK YLCDAYQCAD VIWQYGLLKK GYGLCHGSAG NAYAFLTLYN LTQDMKYLYR ACKFAEWCLE YGEHGCRTPD TPFSLFEGMA GTIYFLADLL VPTKARFPAF EL.
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.
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Name :
CHODL HumanDescription:
Chondrolectin Human Recombinant
Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.
Product # :
PRO-1964Price :
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Description
CHODL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 220 amino acids (22-216) and having a molecular mass of 24.6 kDa.CHODL is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CHODL solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Chondrolectin (CHODL) is a type I membrane protein with a carbohydrate recognition domain characteristic of C-type lectins in its extracellular portion. In other proteins, this domain is involved in endocytosis of glycoproteins and exogenous sugar-bearing pathogens. The CHODL protein localizes mainly to the perinuclear region.
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Synonyms
Chondrolectin, Transmembrane Protein MT75, C21orf68, Chromosome 21 Open Reading Frame 68, PRED12, MT75, CHODL.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSFCRRVVS GQKVCFADFK HPCYKMAYFH ELSSRVSFQE ARLACESEGG VLLSLENEAE QKLIESMLQN LTKPGTGISD GDFWIGLWRN GDGQTSGACP DLYQWSDGSN SQYRNWYTDE PSCGSEKCVV MYHQPTANPG LGGPYLYQWN DDRCNMKHNY ICKYEPEINP TAPVEKPYLT NQPGDTHQNV VVTEAGIIPN.
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.
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Name :
VAMP3 HumanDescription:
Synaptobrevin-3 Human Recombinant
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
Product # :
PRO-652Price :
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Shipped with Ice Packs
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Description
VAMP3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 77 amino acids and having a molecular mass of 8.7 kDa.
Source
Escherichia Coli.
Formulation
The VAMP3 protein solution contains 20mM Tris pH-7.5 and 10% glycerol.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
VAMP3 is present in recycling endosomes and endosome-derived vesicles. VAMP3 has been implicated in recycling of transferrin receptors to the plasma membrane, secretion of alpha-granules in platelets, recycling of T-cell receptors to the immunological synapses, and membrane trafficking during cell migration. VAMP-3 is present in human platelets and necessary for granule secretion. Synaptobrevins are the main components of a protein complex involved in the docking and/or fusion of synaptic vesicles with the presynaptic membrane. VAMP3 high homology to other VAMPs in its broad tissue distribution and subcellular localization is shown to be the human equivalent of the rodent cellubrevin. In platelets the protein resides on a compartment that is not mobilized to the plasma membrane on calcium or thrombin stimulation.
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Synonyms
VAMP3, VAMP-3, Cellubrevin, Vesicle-Associated Membrane Protein 3, Synaptobrevin-3, CEB, SYB3.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MSTGPTAATG SNRRLQQTQN QVDEVVDIMR VNVDKVLERD QKLSELDDRA DALQAGASQF ETSAAKLKRK YWWKNCK.
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.
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Name :
MAPK9 HumanDescription:
Mitogen-Activated Protein Kinase 9 Human Recombinant
Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.
Product # :
PKA-039Price :
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Shipped with Ice Packs
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Description
MAPK9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 406 amino acids (1-382 a.a) and having a molecular mass of 46.6kDa.MAPK9 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MAPK9 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.1M NaCl, 10% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Mitogen-activated protein kinase 9 (MAPK9) belongs to the MAP kinase family. MAP kinases function as an integration point for numerous biochemical signals, and are involved in a broad variety of cellular processes such as proliferation, differentiation, transcription regulation and development. MAPK9 targets specific transcription factors, and consequently mediates immediate-early gene expression in response to diverse cell stimuli. As an active dimer, MAPK9 can translocate to the nucleus and control transcription through its effects on c-Jun, ATF-2, and other transcription factors. MAPK9 blocks the ubiquitination of tumor suppressor p53, and so it increases the stability of p53 in nonstressed cells.
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Synonyms
Mitogen-activated protein kinase 9, MAP kinase 9, MAPK 9, JNK-55, Stress-activated protein kinase 1a, SAPK1a, Stress-activated protein kinase JNK2, c-Jun N-terminal kinase 2, MAPK9, JNK2, PRKM9, SAPK, p54a, JNK2A, JNK2B, JNK2BETA, p54aSAPK, JNK2ALPHA.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSDSKC DSQFYSVQVA DSTFTVLKRY QQLKPIGSGA QGIVCAAFDT VLGINVAVKK LSRPFQNQTH AKRAYRELVL LKCVNHKNII SLLNVFTPQK TLEEFQDVYL VMELMDANLC QVIHMELDHE RMSYLLYQML CGIKHLHSAG IIHRDLKPSN IVVKSDCTLK ILDFGLARTA CTNFMMTPYV VTRYYRAPEV ILGMGYKENV DIWSVGCIMG ELVKGCVIFQ GTDHIDQWNK VIEQLGTPSA EFMKKLQPTV RNYVENRPKY PGIKFEELFP DWIFPSESER DKIKTSQARD LLSKMLVIDP DKRISVDEAL RHPYITVWYD PAEAEAPPPQ IYDAQLEERE HAIEEWKELI YKEVMDWEER SKNGVVKDQP SAQMQQ.
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.
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Name :
4 1BBL Human, HisDescription:
4-1BB Ligand Human Recombinant, His Tag
CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.
Product # :
CYT-649Price :
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Shipped with Ice Packs
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- sds-page
Description
TNFSF9 Human Recombinant fused to 37 amino acids His tag at N-terminus produced in E.Coli is a single, non-glycosylated polypeptide chain containing 222 amino acids (71-254 a.a.) and having a molecular mass of 23.8 kDa. The TNFSF9 37 aa His tag fusion protein is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant 4-1BBL solution (1mg/ml) contains 20mM Tris-HCl buffer pH-8, 100mM NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE
sds-page
More Info
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Introduction
4-1BBL is a transmembrane cytokine that is part of the tumor necrosis factor (TNF) ligand family. 4-1BBL is a bidirectional signal transducer that performs as a ligand for TNFRSF9, which is a costimulatory receptor molecule in T lymphocytes. TNFSF9 and its TNFRSF9 take part in the antigen presentation development and in the generation of cytotoxic T cells. 4-1BBR is absent from resting T lymphocytes but rapidly expressed upon antigenic stimulation. TNFSF9 reactivates anergic T lymphocytes as well as promoting T lymphocyte proliferation. 4-1BB Ligand is needed for the optimal CD8 responses in CD8 T cells. 4-1BBL is expressed in carcinoma cell lines, and is thought to be involved in T cell-tumor cell interaction. 4-1BBL is expressed by activated B cells, macrophages, dendritic cells, activated T cells, neurons and astrocytes. The interaction of 4-1BB with TNFRSF9 strongly regulates immunity and has been proposed to preferentially control T cell responses based on studies in various murin
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Synonyms
CD137L, CD137-L, 4-1BBL, 4-1BB Ligand, TNFSF9, Tumor Necrosis Factor (ligand) Superfamily Member 9.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MRGSHHHHHH GMASMTGGQQ MGRDLYDDDD KDRWGSHMRE GPELSPDDPA GLLDLRQGMF AQLVAQNVLL IDGPLSWYSD PGLAGVSLTGGLSYKEDTKE LVVAKAGVYY VFFQLELRRV VAGEGSGSVS LALHLQPLRS AAGAAALALT VDLPPASSEA RNSAFGFQGR LLHLSAGQRL GVHLHTEARA RHAWQLTQGA TVLGLFRVTP EIPAGLPSPR SE.
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.
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Name :
LIF HumanDescription:
Leukemia Inhibitory Factor Human Recombinant
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
Product # :
CYT-644Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Leukemia Inhibitory Factor (LIF) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19.7kDa. The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Leukemia Inhibitory Factor (LIF) was lyophilized from a concentrated (1mg/ml) sterile solution containing 1xPBS pH 7.4.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 100,000,000IU/mg.More Info
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Introduction
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
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Synonyms
CDF, HILDA, D-FACTOR, Differentiation- stimulating factor, Melanoma-derived LPL inhibitor, MLPLI, Emfilermin, Leukemia inhibitory factor, LIF, DIA.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Leukemia Inhibitory Factor (LIF) although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Leukemia Inhibitory Factor (LIF) 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.
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Solubility
It is recommended to reconstitute the lyophilized Leukemia Inhibitory Factor (LIF) in sterile water not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF.
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Background
Leukemia Inhibitory Factor (LIF) Background
Leukemia Inhibitory Factor (LIF) is a cytokine within the interleukin-6 family. It is influential in the hypothalamus and involved in energy balance.
LIF stimulates ACTH secretion and affects the stress and immune response in the body. Administration of LIF has been shown to correct low plasma ACTH and repair hypothalamic-pituitary-adrenal (HPA) axis responses.
Function and Applications of LIF
LIF prevents the proliferation of myeloid leukemia cells by inducing their terminal differentiation. Beyond cancer, LIF influences bone metabolism, embryogenesis, and inflammation.
Moreover, it supports the self-renewal of stem cells in culture by activating Stat3, thus preventing spontaneous differentiation, and is studied for potential benefits in fertility treatments.
Structure and Interactions
LIF's structure consists of a four alpha-helix bundle similar to other hematopoietic cytokines. It interacts with components such as the ciliary neurotrophic factor (CNTF) through multimeric receptors, influencing both cytokine's effects on cells. This interaction is crucial for forming high-affinity binding sites that mediate their biological activities.
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.
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Name :
SNCA 1-95, HumanDescription:
Alpha-Synuclein 1-95 Human Recombinant
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
Product # :
PRO-2625Price :
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Shipped with Ice Packs
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Description
SNCA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (1-95 a.a.) and having a molecular mass of 9.3kDa.SNCA is purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SNCA protein solution (1mg/ml) containing 20 mM Tris-HCl buffer (pH 7.5) and 0.1 M NaCl.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Alpha-synuclein or SNCA is a synuclein protein. SNCA mainly found in the brain, small concentration of the protein can also be located in other tissues such as heart and muscle. When looking in the brain tissue, SNCA is located in the end of the neuron, in an area called presynaptic terminal. In the presynaptic terminal SNCA has interaction with phospholipids & other proteins. Neurotransmitters are released from the synaptic vesicles in the Presynaptic terminals and act as messengers. Once released, the neurotransmitters send signals across the neurons that are crucial for the brain’s operation.
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Synonyms
SNCA, NACP, PARK1, alpha-Synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Alpha synuclein, Alpha-synuclein isoform NACP140, alphaSYN, MGC105443, MGC110988, MGC127560, MGC64356, Non A beta component of AD amyloid, Non A4 component of amyloid precursor, Non-A-beta component of alzheimers disease amyloid, precursor of PARK 1, PARK 4, PARK4, Parkinson disease familial 1, PD 1, PD1, Synuclein alpha.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFV
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.
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Name :
PROCR Human, Sf9Description:
Protein-c Receptor Human Recombinant, Sf9
Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA.
Product # :
PRO-2438Price :
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Description
PROCR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 435 amino acids (18-210a.a.) and having a molecular mass of 49.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa). PROCR is expressed with a 242 amino acids hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
PROCR protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Protein-c Receptor (PROCR) is a receptor for activated protein C, a serine protease activated by and involved in the blood coagulation pathway. The PROCR protein is an N-glycosylated type I membrane protein which enhances the activation of protein C. PROCR gene mutations are linked with venous thromboembolism and myocardial infarction, as well as with late fetal loss during pregnancy. In addition, PROCR may have a role in malarial infection and has been linked with cancer.
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Synonyms
Protein C Receptor, CD201, APC Receptor, EPCR, Centrocyclin, CCD41, CCCA.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPSQDASDG LQRLHMLQIS YFRDPYHVWY QGNASLGGHL THVLEGPDTN TTIIQLQPLQ EPESWARTQS GLQSYLLQFH GLVRLVHQER TLAFPLTIRC FLGCELPPEG SRAHVFFEVA VNGSSFVSFR PERALWQADT QVTSGVVTFT LQQLNAYNRT RYELREFLED TCVQYVQKHI SAENTKGSQT SRSYTSLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
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.
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Name :
ME2 HumanDescription:
Malic Enzyme 2 Human Recombinant
Malic enzyme 2 NAD(+)-dependent mitochondrial, NAD-ME, ODS1, Malate Dehydrogenase, NAD-dependent malic enzyme mitochondrial, pyruvic-malic carboxylase, Malic enzyme 2, EC 1.1.1.38, EC 1.1.1.
Product # :
ENZ-376Price :
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Shipped at Room temp
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Description
ME2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 573 amino acids and having a total molecular mass of 64.4kDa.ME2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a 0.2µm filtered concentrated solution in 20mM Tris, 150mM NaCl, 1mM b-mercaptoethanol, 1mM EDTA, pH8.0.
Purity
Greater than 95.0% as determined by
(a) Analysis by HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
ME2 catalyzes the oxidative decarboxylation of malate to pyruvate, malat + NAD(P)+? pyruvate + CO2 + NAD(P)H+, and is found both in eukaryotic and prokaryotic cells. Three different isoforms of ME are known to be in mammalian tissues: a strictly cytosolic NADP+-dependent enzyme, an NADP+-dependent mitochondriail isoform, and a mitochondrial isoenzyme that is able to use both NAD+ and NADP+ but is more effective with NAD+. The mammalian isoforms size is about 62-64 kDa. A native size of 240,000 Da proposes a tetrameric structure for the active enzyme.
Mitochondrial NAD+-dependent ME 2 activity is seen in tissues that experience many cell divisions, like spleen, thymus, and the basal cells of the small intestinal mucosa. ME2 is also expressed all through the rapid cleavage stages of early Xenopus development. Activity for this isoform is low or nonexistent in brain, muscle, and normal and regenerating liver tissue from rat but was observed in rat adrenal cortex, pigeon and human skeletal muscle, and in heart muscle of some species. In addition, it is expressed in mitochondria of all tumor cells inspected to detain ascites tumors, hepatoma cells, and a variety of other tumors and transformed cell lines. -
Synonyms
Malic enzyme 2 NAD(+)-dependent mitochondrial, NAD-ME, ODS1, Malate Dehydrogenase, NAD-dependent malic enzyme mitochondrial, pyruvic-malic carboxylase, Malic enzyme 2, EC 1.1.1.38, EC 1.1.1.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized ME2 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ME2 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
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Solubility
It is recommended to reconstitute the lyophilized ME2 in sterile 18M-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MLHIKEKGKPLMLNPRTNKGMAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLK
KMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGL
FISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTAC
AGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYG
RNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEH
KILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQ
EPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPT
AQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILC
NTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAF
RYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITEHHHHHH.
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.
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Name :
YY1 HumanDescription:
YY1 Transcription Factor Human Recombinant
YY1 transcription factor, YY1, DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, Transcriptional repressor protein YY1, Delta transcription factor, Yin and yang 1, INO80 complex subunit S, YY-1.
Product # :
PRO-2108Price :
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Description
YY1 Human Recombinant produced in E. coli is a single polypeptide chain containing 437 amino acids (1-414) and having a molecular mass of 47.1kDa.YY1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YY1 solution (0.25mg/1ml) contains PBS, 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
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Introduction
YY1 Transcription Factor, also known as YY1, is a part of the GLI-Kruppel class of zinc finger proteins. YY1 has a positive and negative effect on a various cellular and viral genes by binding to sites overlapping the transcription start site. YY1 leads histone deacetylases and histone acetyltransferases to a promoter in order to activate or repress the promoter.
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Synonyms
YY1 transcription factor, YY1, DELTA, INO80S, NF-E1, UCRBP, YIN-YANG-1, Transcriptional repressor protein YY1, Delta transcription factor, Yin and yang 1, INO80 complex subunit S, YY-1.
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Physical Appearance
Sterile Filtered clear solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMASGDTL YIATDGSEMP AEIVELHEIE VETIPVETIE TTVVGEEEEE DDDDEDGGGG DHGGGGGHGH AGHHHHHHHH HHHPPMIALQ PLVTDDPTQV HHHQEVILVQ TREEVVGGDD SDGLRAEDGF EDQILIPVPA PAGGDDDYIE QTLVTVAAAG KSGGGGSSSS GGGRVKKGGG KKSGKKSYLS GGAGAAGGGG ADPGNKKWEQ KQVQIKTLEG EFSVTMWSSD EKKDIDHETV VEEQIIGENS PPDYSEYMTG KKLPPGGIPG IDLSDPKQLA EFARMKPRKI KEDDAPRTIA CPHKGCTKMF RDNSAMRKHL HTHGPRVHVC AECGKAFVES SKLKRHQLVH TGEKPFQCTF EGCGKRFSLD FNLRTHVRIH TGDRPYVCPF DGCNKKFAQS TNLKSHILTH AKAKNNQ.
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.
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Name :
GEMIN6 HumanDescription:
Gem-Associated Protein 6 Human Recombinant
Gem-associated protein 6, Gemin-6, SIP2, GEMIN6.
Product # :
PRO-1394Price :
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Description
GEMIN6 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 190 amino acids (1-167a.a) and having a molecular mass of 21.9kDa. GEMIN6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
GEMIN6 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Gem-Associated Protein 6 (GEMIN6) is a member of a large macromolecular complex, localized to both the cytoplasm and the nucleus, which takes part in the cytoplasmic assembly of small nuclear ribonucleoproteins (snRNPs). SMN, GEMIN2, GEMIN3, GEMIN4, and GEMIN5 are additional members of this complex.
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Synonyms
Gem-associated protein 6, Gemin-6, SIP2, GEMIN6.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSEWMKK GPLEWQDYIY KEVRVTASEK NEYKGWVLTT DPVSANIVLV NFLEDGSMSV TGIMGHAVQT VETMNEGDHR VREKLMHLFT SGDCKAYSPE DLEERKNSLK KWLEKNHIPI TEQGDAPRTL CVAGVLTIDP PYGPENCSSS NEIILSRVQD LIEGHLTASQ.
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.
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Name :
CD84 Human, Sf9Description:
CD84 Human Recombinant, Sf9
CD84 Molecule, Signaling Lymphocytic Activation Molecule 5, Leukocyte Differentiation Antigen CD84, CD84 Antigen (Leukocyte Antigen), Cell Surface Antigen MAX.3, Hly9-Beta, SLAMF5, Leucocyte Differentiation Antigen CD84, Leukocyte Antigen CD84, SLAM Family Member 5, CD84 Antigen, HCD84, MCD84, LY9B, SLAM family member 5, Cell surface antigen MAX.3, Hly9-beta, Leukocyte differentiation antigen CD84, Signaling lymphocytic activation molecule 5.
Product # :
PRO-2409Price :
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Description
CD84 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 213 amino acids (22-225 a.a.) and having a molecular mass of 23.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CD84 is expressed with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CD84 protein solution (0.5mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 95% as determined by SDS-PAGE.
More Info
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Introduction
CD84 belongs to the signaling lymphocyte activation molecule (SLAM) family which forms a subset of the greater CD2 cell-surface receptor Ig superfamily. CD84, a membrane glycoprotein, is a homophilic adhesion molecule found in various immune cells types and takes part in regulating receptor-mediated signaling in those cells.
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Synonyms
CD84 Molecule, Signaling Lymphocytic Activation Molecule 5, Leukocyte Differentiation Antigen CD84, CD84 Antigen (Leukocyte Antigen), Cell Surface Antigen MAX.3, Hly9-Beta, SLAMF5, Leucocyte Differentiation Antigen CD84, Leukocyte Antigen CD84, SLAM Family Member 5, CD84 Antigen, HCD84, MCD84, LY9B, SLAM family member 5, Cell surface antigen MAX.3, Hly9-beta, Leukocyte differentiation antigen CD84, Signaling lymphocytic activation molecule 5.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADPKDSEIFT VNGILGESVT FPVNIQEPRQ VKIIAWTSKT SVAYVTPGDS ETAPVVTVTH RNYYERIHAL GPNYNLVISD LRMEDAGDYK ADINTQADPY TTTKRYNLQI YRRLGKPKIT QSLMASVNST CNVTLTCSVE KEEKNVTYNW SPLGEEGNVL QIFQTPEDQE LTYTCTAQNP
VSNNSDSISA RQLCADIAMG FRTHHTGHHH HHH.
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.
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Name :
GSTM1 Human, Sf9Description:
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-1092Price :
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Description
GSTM1 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain (1-218a.a.) fused to a 9 aa His Tag at C-terminus containing 227 amino acids and having a molecular mass of 26.8kDa. GSTM1 shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
GSTM1 protein solution (0.5mg/ml) contains 40% glycerol, 0.2M NaCl, 2mM DTT and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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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.
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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.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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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.
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.
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Name :
REG4 Human, Sf9Description:
Regenerating Islet-Derived 4 Human Recombinant, Sf9
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
Product # :
PRO-2595Price :
Quantity :
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Shipped with Ice Packs
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Description
REG4 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (23-158 a.a.) and fused to a 9 aa His Tag at C-terminus containing a total of 145 amino acids and having a molecular mass of 17kDa.REG4 shows multiple bands between 13.5-18kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
REG4 protein solution (0.25mg/ml) contains 10% glycerol & Phosphate buffered saline (pH7.4).
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
REG protein was shown to be stimulated during the regeneration of pancreatic islets. Since then, many Reg-related proteins have been identified in humans and other animals. In human, the four REG family genes, i.e., REG 1 alpha, REG 1 beta, REG-related sequence (RS) and HIP/PAP, have so far been isolated. These Reg-related proteins are classified into four subfamilies according to their amino-acid sequences, but they share a similar structure and physiological function. Reg protein is a growth factor for pancreatic beta cells and also suggests that the administration of Reg protein could be used as another therapeutic approach for diabetes mellitus. Human REG cDNA which encodes a 166-amino acid protein with a 22-amino acid signal peptide. The amino acid sequence of human REG protein has 68% homology to that of rat Reg protein.
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Synonyms
Regenerating islet-derived protein 4, Reg IV, REG-like protein, Gastrointestinal secretory protein, REG4, GISP, RELP.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ADPDIIMRPS CAPGWFYHKS NCYGYFRKLR NWSDAELECQ SYGNGAHLAS ILSLKEASTI
AEYISGYQRS QPIWIGLHDP QKRQQWQWID GAMYLYRSWS GKSMGGNKHC AEMSSNNNFL TWSSNECNKR QHFLCKYRPH HHHHH
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.
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Name :
CHMP5 HumanDescription:
Charged Multivesicular Body Protein 5 Human Recombinant
Charged Multivesicular Body Protein 5, SNF7 Domain-Containing Protein 2, Chromosome 9 Open Reading Frame 83, Chromatin-Modifying Protein 5, Apoptosis-Related Protein PNAS-2, Vacuolar Protein Sorting-Associated Protein 60, Chromatin Modifying Protein 5, HSPC177, PNAS-2, HVps60, SNF7DC2, CGI-34, C9orf83.
Product # :
PRO-1232Price :
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Description
CHMP5 Human Recombinant produced in E. coli is a single polypeptide chain containing 243 amino acids (1-219) and having a molecular mass of 27.0 kDa.CHMP5 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The CHMP5 solution (0.25mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl and 30% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
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Introduction
Charged Multivesicular Body Protein 5 (CHMP5) is a member of the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins comprise the ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and development of endocytic multivesicular bodies (MVBs). Certain CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP the CHMP1A, is essential for both MVB formation and regulation of cell cycle progression.
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Synonyms
Charged Multivesicular Body Protein 5, SNF7 Domain-Containing Protein 2, Chromosome 9 Open Reading Frame 83, Chromatin-Modifying Protein 5, Apoptosis-Related Protein PNAS-2, Vacuolar Protein Sorting-Associated Protein 60, Chromatin Modifying Protein 5, HSPC177, PNAS-2, HVps60, SNF7DC2, CGI-34, C9orf83.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSH MNRLFG KAKPKAPPPS LTDCIGTVDS RAESIDKKIS RLDAELVKYK DQIKKMREGP AKNMVKQKAL RVLKQKRMYE QQRDNLAQQS FNMEQANYTI QSLKDTKTTV DAMKLGVKEM KKAYKQVKID QIEDLQDQLE DMMEDANEIQ EALSRSYGTP ELDEDDLEAE LDALGDELLA DEDSSYLDEA ASAPAIPEGV PTDTKNKDGV LVDEFGLPQI PAS
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.
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Name :
FCGR3A Human, Sf9Description:
CD16a Human Recombinant, Sf9
Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.
Product # :
PRO-2360Price :
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Description
FCGR3A Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 200 amino acids (18-208 a.a.) and having a molecular mass of 22.8kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).FCGR3A is fused with a 6 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
FCGR3A protein solution (0.25mg/ml) contains Phosphate buffered saline (pH7.4) and 10% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
Low affinity immunoglobulin gamma Fc region receptor III-A (FCGR3A) is a receptor for the Fc portion of immunoglobulin G, and is involved in the elimination of antigen-antibody complexes from the circulation, as well as other antibody-dependent responses. FCGR3A needs to associate with the gamma subunit of Fc epsilon. The FCGR3A receptor is expressed on natural killer (NK) cells as an integral membrane glycoprotein anchored through a transmembrane peptide, while FCGR3B is expressed on polymorphonuclear neutrophils (PMN) where the receptor is anchored through a phosphatidylinositol (PI) linkage. In addition, FCGR3A is expressed on macrophages, subpopulation of T-cells, immature thymocytes and placental trophoblasts. FCGR3A mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis. FCGR3A gene mutations are linked with susceptibility to recurrent viral infections, susceptibility to systemic lupus erythematosus, and alloimmune neonatal neutropenia.
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Synonyms
Low affinity immunoglobulin gamma Fc region receptor III-A, CD16a antigen, Fc-gamma, RIII-alpha, Fc-gamma RIII, Fc-gamma RIIIa, FcRIII, FcRIIIa, FcR-10, IgG Fc receptor III-2, CD16a, FCGR3A, FCG3, FCGR3, IGFR3, CD16, FCGRIII.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
ADPMRTEDLP KAVVFLEPQW YRVLEKDSVT LKCQGAYSPE DNSTQWFHNE SLISSQASSY FIDAATVDDS GEYRCQTNLS TLSDPVQLEV HIGWLLLQAP RWVFKEEDPI HLRCHSWKNT ALHKVTYLQN GKGRKYFHHN SDFYIPKATL KDSGSYFCRG LFGSKNVSSE TVNITITQGL AVSTISSFFP PGYQHHHHHH.
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Background
CD16A, also known as Fc gamma receptor IIIA (FcγRIIIA), is a key receptor involved in immune responses and antibody-dependent cell-mediated cytotoxicity (ADCC). This research paper aims to explore the structure, function, and therapeutic implications of CD16A, shedding light on its diverse roles in immune regulation and targeted therapies.
CD16A is a transmembrane protein expressed primarily on natural killer (NK) cells, macrophages, and a subset of activated neutrophils. It interacts with the Fc portion of immunoglobulin G (IgG) antibodies, thereby mediating ADCC. Upon binding to IgG-coated target cells, CD16A triggers intracellular signaling cascades that initiate immune effector functions, leading to target cell destruction.
The structure of CD16A consists of an extracellular domain responsible for IgG binding, a transmembrane domain, and an intracellular domain involved in signal transduction. Genetic polymorphisms in CD16A have been identified, leading to variations in its affinity for IgG subclasses and influencing immune responses and disease susceptibility.
The function of CD16A extends beyond its role in ADCC. It also participates in immune cell activation, cytokine production, and regulation of immune responses. CD16A engagement on NK cells can trigger cytotoxicity and cytokine release, contributing to antiviral and antitumor immune responses. Moreover, CD16A-mediated cross-talk between immune cells modulates immune surveillance and inflammation.
Therapeutically, CD16A has emerged as a potential target for immunotherapy. Monoclonal antibodies designed to enhance CD16A-mediated ADCC have shown promising results in the treatment of cancer. By engaging CD16A on immune effector cells, these antibodies facilitate targeted cell killing and tumor eradication. Additionally, CD16A-based immunotherapies have been explored in infectious diseases and autoimmune disorders.
The availability of CD16A human recombinant proteins has facilitated extensive research and drug development efforts. Recombinant CD16A proteins serve as valuable tools for studying CD16A interactions, optimizing immunotherapeutic strategies, and evaluating the efficacy of novel therapeutic agents.
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.
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Name :
PMM1 HumanDescription:
Phosphomannomutase 1 Human Recombinant
Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.
Product # :
ENZ-023Price :
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Description
PMM1 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 282 amino acids (1-262 a.a.) and having a molecular mass of 31.9kDa. The PMM1 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The PMM1 solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 2mM DTT, 100mM NaCl and 0.1mM PMSF.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Phosphomannomutase 1 (PMM1) is an enzyme involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions. PMM1 catalyzes the conversion between D-mannose 6-phosphate and D-mannose 1-phosphate which is a substrate for GDP-mannose synthesis. GDP-mannose is used for the synthesis of dolichol-phosphate-mannose, which is crucial for N-linked glycosylation and accordingly the secretion of several glycoproteins as well as for the synthesis of glycosyl-phosphatidyl-inositol (GPI) anchored proteins. Additionally, PMM1 may be responsible for the degradation of glucose-1,6-bisphosphate in ischemic brain.
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Synonyms
Phosphomannomutase 1, PMM 1, PMMH-22, PMM1, PMMH22, Sec53.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAVTAQAARR KERVLCLFDV DGTLTPARQK IDPEVAAFLQ KLRSRVQIGV VGGSDYCKIA EQLGDGDEVI EKFDYVFAEN GTVQYKHGRL LSKQTIQNHL GEELLQDLIN FCLSYMALLR LPKKRGTFIE FRNGMLNISP IGRSCTLEER IEFSELDKKE KIREKFVEAL KTEFAGKGLR FSRGGMISFD VFPEGWDKRY CLDSLDQDSF DTIHFFGNET SPGGNDFEIF ADPRTVGHSV VSPQDTVQRC REIFFPETAH EA.
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.
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Name :
GATM HumanDescription:
Glycine Amidinotransferase Human Recombinant
Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.
Product # :
ENZ-583Price :
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Description
GATM Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 410 amino acids (38-423) and having a molecular mass of 46.9kDa (Molecular size on SDS-PAGE will appear higher).GATM is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
The GATM solution (1mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 10% glycerol and 200mM NaCl.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
Glycine amidinotransferase mitochondrial (GATM) is a mitochondrial enzyme which is a member of the amidinotransferase family. The GATM enzyme is involved in creatine biosynthesis, where it catalyzes the transfer of a guanido group from L-arginine to glycine, resulting in guanidinoacetic acid, the immediate precursor of creatine, which has an imperative role in energy metabolism in muscle tissues. GATM is significant in embryonic and central nervous system development. GATM gene mutations cause arginine:glycine amidinotransferase deficiency, an inborn error of creatine synthesis characterized by mental retardation, language impairment, and behavioral disorders.
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Synonyms
Glycine amidinotransferase, mitochondrial, L-arginine:glycine amidinotransferase, Transamidinase, GATM, AGAT, AT.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSTQAAT ASSRNSCAAD DKATEPLPKD CPVSSYNEWD PLEEVIVGRA ENACVPPFTI EVKANTYEKY WPFYQKQGGH YFPKDHLKKA VAEIEEMCNI LKTEGVTVRR PDPIDWSLKY KTPDFESTGL YSAMPRDILI VVGNEIIEAP MAWRSRFFEY
RAYRSIIKDY FHRGAKWTTA PKPTMADELY NQDYPIHSVE DRHKLAAQGK FVTTEFEPCF DAADFIRAGR DIFAQRSQVT NYLGIEWMRR HLAPDYRVHI ISFKDPNPMH IDATFNIIGP GIVLSNPDRP CHQIDLFKKA GWTIITPPTP IIPDDHPLWM SSKWLSMNVL MLDEKRVMVD
ANEVPIQKMF EKLGITTIKV NIRNANSLGG GFHCWTCDVR RRGTLQSYLD.
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.
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Name :
MAPT HumanDescription:
Microtubule-Associated Protein Tau Human Recombinant
TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.
Product # :
PRO-295Price :
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Shipped with Ice Packs
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Description
MAPT Recombinant Human (Isoform-4) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 372 amino acids (1-352 a.a.) and having a molecular mass of 38.9 kDa (Real molecular weight on SDS-PAGE will be shift up). The MAPT is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The MAPT solution (0.5mg/ml) contains 20mM Tris-HCl pH-8, 1mM DTT, 0.2M NaCl & 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
MAPT is a neuronal microtubule associated protein localized mostly on axons.
MAPT promotes tubulin polymerisation and stabilizes microtubules, however it also serves to connect certain signalling pathways to the cytoskeleton. MAPT, in its hyperphosphorylated form, is the main part of paired helical filaments (PHF) and neurofibrillary lesions in Alzheimer''s disease (AD) brain. -
Synonyms
TAU, DDPAC, FTDP-17, MAPTL, MSTD, MTBT1, MTBT2, PPND.
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Physical Appearance
Sterile filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MAEPRQEFEV MEDHAGTYGL GDRKDQGGYT MHQDQEGDTD AGLKAEEAGI GDTPSLEDEA AGHVTQARMV SKSKDGTGSD DKKAKGADGK TKIATPRGAA PPGQKGQANA TRIPAKTPPA PKTPPSSGEP PKSGDRSGYS SPGSPGTPGS RSRTPSLPTP PTREPKKVAV VRTPPKSPSS AKSRLQTAPV PMPDLKNVKS KIGSTENLKH QPGGGKVQIV YKPVDLSKVT SKCGSLGNIH HKPGGGQVEV KSEKLDFKDR VQSKIGSLDN ITHVPGGGNK KIETHKLTFR ENAKAKTDHG AEIVYKSPVV SGDTSPRHLS NVSSTGSIDM VDSPQLATLA DEVSASLAKQ GL.
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.
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Name :
AHCY Human, Sf9Description:
Adenosylhomocysteinase Human Recombinant, Sf9
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
Product # :
ENZ-1034Price :
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Description
AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AHCY protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
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Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH 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.
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Name :
CDKN1A HumanDescription:
Cyclin-Dependent Kinase Inhibitor 1A Human Recombinant
Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.
Product # :
PKA-043Price :
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Description
CDKN1A Human Recombinant produced in E. coli is a single polypeptide chain containing 184 amino acids (1-164) and having a molecular mass of 20.2 kDa.CDKN1A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The CDKN1A solution contains 20mM Tris-HCl buffer (pH 8.0), 2M Urea, 0.1M NaCl and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
CDKN1A holds a key part in the cellular response to DNA mutation. CDKN1A overexpression causes cell cycle to stop. When collaborating with CDK2 complexes, CDKN1A aids to prevent kinase activity and inhibits progression through G1/S. Nevertheless, CDKN1A can additionally increase assembly and activity in complexes of CDK4 or CDK6 and cyclin D. CDKN1A is a vital intermediary by which p53/TP53 facilitates its part as an inhibitor of cellular proliferation as a reaction to DNA impairment.
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Synonyms
Cyclin-Dependent Kinase Inhibitor 1A (P21, Cip1), Melanoma Differentiation Associated Protein 6, Wild-Type P53-Activated Fragment 1, CDK-Interaction Protein 1, DNA Synthesis Inhibitor, CDK-Interacting Protein 1, CDKN1, P21Cip1/Waf1, MDA6, P21CIP1, CAP20, WAF1, CIP1, PIC1, P21, SDI1.
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Physical Appearance
Sterile Filtered colorless solution.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MSEPAGDVRQ NPCGSKACRR LFGPVDSEQL SRDCDALMAG CIQEARERWN FDFVTETPLE GDFAWERVRG LGLPKLYLPT GPRRGRDELG GGRRPGTSPA LLQGTAEEDH VDLSLSCTLV PRSGEQAEGS PGGPGDSQGR KRRQTSMTDF YHSKRRLIFS KRKP.
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.