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1000 results found for “stathmin”
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Name :
SEPT2 HumanDescription:
Septin-2 Human Recombinant
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-5.
Product # :
PRO-255Price :
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Shipped with Ice Packs
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Description
SEPT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 381 amino acids (1-361 a.a.) and having a molecular mass of 43.6kDa. SEPT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SEPT2 solution (0.25mg/1ml) containing 20mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SEPT2 is a GTPase which is mandatory for cytokinesis and related to exocytosis. Septin-2 protein is able to hetero-oligomerize with Septin6, 7 and in addition takes part in the organization of new growth in organisms. SEPT2 is associated with a Tau-based paired helical filament core and contributes to the creation of neurofibrillary tangle as integral constituents of paired helical filaments.
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Synonyms
Septin 2, DIFF6, NEDD5, hNedd5, Pnutl3, NEDD-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
MGSSHHHHHH SSGLVPRGSH MSKQQPTQFI NPETPGYVGF ANLPNQVHRK SVKKGFEFTL MVVGESGLGK STLINSLFLT DLYPERVISG AAEKIERTVQ IEASTVEIEE RGVKLRLTVV DTPGYGDAIN CRDCFKTIIS YIDEQFERYL HDESGLNRRH IIDNRVHCCF YFISPFGHGL KPLDVAFMKA IHNKVNIVPV IAKADTLTLK ERERLKKRIL DEIEEHNIKI YHLPDAESDE DEDFKEQTRL LKASIPFSVV GSNQLIEAKG KKVRGRLYPW GVVEVENPEH NDFLKLRTML ITHMQDLQEV TQDLHYENFR SERLKRGGRK VENEDMNKDQ ILLEKEAELR RMQEMIARMQ AQMQMQMQGG DGDGGALGHH V.
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 :
VSTM2L HumanDescription:
V-Set and Transmembrane Domain Containing 2 Like Human Recombinant
V-set and transmembrane domain-containing protein 2-like protein, VSTM2L, C20orf102, dJ1118M15.2.
Product # :
PRO-1018Price :
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Shipped with Ice Packs
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Description
VSTM2L Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 205 amino acids (25-204 a.a.) and having a molecular mass of 22.6kDa. VSTM2L is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
VSTM2L protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl,1mM DTT and 0.1mM PMSF.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
V-set and transmembrane domain containing 2 (VSTM2L) is a novel modulator of HN neuroprotective activity. VSTM2L colocalizes with HN in distinct brain areas as well as in primary cultured neurons, where it plays a part in the modulation of neuronal viability. When tested in HN neuroprotection bioassays, VSTM2L acts as a potent antagonist of HN neuroprotective activity. The VSTM2L protein is the first example of a secreted antagonist of HN and may have a role in the modulation of HN biological functions.
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Synonyms
V-set and transmembrane domain-containing protein 2-like protein, VSTM2L, C20orf102, dJ1118M15.2.
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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 MGSHMTRPAG HAPWDNHVSG HALFTETPHD MTARTGEDVE MACSFRGSGS PSYSLEIQWW YVRSHRDWTD KQAWASNQLK ASQQEDAGKE ATKISVVKVV GSNISHKLRL SRVKPTDEGS YECRVIDFSD GKARHHKVKA YLRVQPGENS VLHLPEAPPA APAPPPPKPG KELRKRSVDQ EACSL.
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 :
Lamin-A HumanDescription:
Lamin-A Human Recombinant
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
Product # :
PRO-690Price :
Quantity :
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Description
Recombinant Human Lamin A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 645 amino acids and having a molecular mass of 70 kDa. Lamin-A protein is fused to a 6xHis tag at N-terminus and purified by conventional chromatography techniques.
Source
Escherichia Coli.
Formulation
The Lamin-A Protein solution (0.9mg/ml) contains 20mM phosphate buffer pH 7.0, 500mM NaCl, 1mM DTT, 1.5mM EDTA and 20% (v/v) Glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Lamin-A is a major component of the nuclear lamina, a dynamic meshwork located just under the nuclear envelope and it is encoded by lamin A/C gene (LMNA).
Lamin-A is synthesized as Prelamin A, a longer precursor that in vivo goes through a serial post-translational modifications that lead to mature Lamin A.
Diverse mutations in the Lamin A/C gene are associated with different diseases that are collectively called laminophaties, including Emery-Dreifuss muscular dystrophy, familiar partial lipodystrophy, limb girdle muscular dystrophy, dilated cardiomyopathy, Charcot-Marie-Tooth disease, and Hutchinson-Gilford progeria syndrome. -
Synonyms
Prelamin-A/C, LMNA, LMN1, Lamin-A/C, 70 kDa lamin, Renal carcinoma antigen NY-REN-32, FPL, IDC, LFP, CDDC, EMD2, FPLD, HGPS, LDP1, LMNC, PRO1, CDCD1, CMD1A, FPLD2, LMNL1, CMT2B1, LGMD1B.
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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. Avoid multiple freeze-thaw cycles.
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Amino Acid Sequence
HHHHHH-METPSQRRATRSGAQASSTPLSPTRITRLQEKEDLQELNDRLAVYIDRVHSLETENAGLRLRITES
EEVVSREVSGIKAAYEAELGDARKTLDSVAKERARLQLELSKVREEFKELKARNTKKEGDLIAAQA
RLKDLEALLNSKEAALSTALSEKRTLEGELHDLRGQVAKLEAALGEAKKQLQDEMLRRVDAENRL
QTMKEELDFQKNIYSEELRETKRRHETRLVEIDNGKQREFESRLADALQELRAQHEDQVEQYKKE
LEKTYSAKLDNARQSAERNSNLVGAAHEELQQSRIRIDSLSAQLSQLQKQLAAKEAKLRDLEDSLA
RERDTSRRLLAEKEREMAEMRARMQQQLDEYQELLDIKLALDMEIHAYRKLLEGEEERLRLSPSP
TSQRSRGRASSHSSQTQGGGSVTKKRKLESTESRSSFSQHARTSGRVAVEEVDEEGKFVRLRN
KSNEDQSMGNWQIKRQNGDDPLLTYRFPPKFTLKAGQVVTIWAAGAGATHSPPTDLVWKAQNT
WGCGNSLRTALINSTGEEVAMRKLVRSVTVVEDDEDEDGDDLLHHHHGSHCSSSGDPAEYNLRS
RTVLCGTCGQPADKASASGSGAQVGGPISSGSSASSVTVTRSYRSVGGSGGGSFGDNLVTRS
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 :
SMCP HumanDescription:
Sperm Mitochondria-Associated Cysteine-Rich Protein Human Recombinant
Sperm Mitochondria-Associated Cysteine-Rich Protein, MCSP, MCS, Mitochondrial Capsule Selenoprotein, HSMCSGEN1, Sperm Mitochondrial-Associated Cysteine-Rich Protein.
Product # :
PRO-1719Price :
Quantity :
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Shipped with Ice Packs
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Description
SMCP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 139 amino acids (1-116 a.a) and having a molecular mass of 15.2kDa (Molecular size on SDS-PAGE will appear higher). SMCP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
SMCP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 20% glycerol, 1mM EDTA and 0.1mM PMSF.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
SMCP is a protein-coding gene. SMCP localizes to the capsule linked with the mitochondrial outer membranes and assumed to function in the organization and stabilization of the helical structure of the sperm's mitochondrial sheath. Sperm mitochondria vary in morphology and subcellular localization from those of somatic cells. They are elongated, flattened, and arranged circumferentially construct a helical coiled sheath in the midpiece of the sperm flagellum. Diseases associated with SMCP include middle ear disease, and hard palate cancer.
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Synonyms
Sperm Mitochondria-Associated Cysteine-Rich Protein, MCSP, MCS, Mitochondrial Capsule Selenoprotein, HSMCSGEN1, Sperm Mitochondrial-Associated Cysteine-Rich Protein.
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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 MGSMCDQTKH SKCCPAKGNQ CCPPQQNQCC QSKGNQCCPP KQNQCCQPKG SQCCPPKHNH CCQPKPPCCI QARCCGLETK PEVSPLNMES EPNSPQTQDK GCQTQQQPHS PQNESRPSK.
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 :
OSM RatDescription:
Oncostatin-M Rat Recombinant
Oncostatin-M, OSM, OncoM.
Product # :
CYT-169Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
OSM Rat Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 214 amino acids and having a molecular mass of 24.3kDa.The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OSM protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH 7.4.
Purity
Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependent stimulation of the proliferation of rat C6 cells is < 5.0 µg/ml, corresponding to a specific activity of > 200 units/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
Oncostatin-M, OSM, OncoM.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
KRGCSSSSPK LLSQLKSQAN ITGNTASLLE PYILHQNLNT LTLRAACTEH PVAFPSEDML RQLSKPDFLS TVHATLGRVW HQLGAFRQQF PKIQDFPELE RARQNIQGIR NNVYCMARLL HPPLEIPEPT QADSGTSRPT TTAPGIFQIK IDSCRFLWGY HRFMGSVGRV FEEWGDGSRR SR RHSPLWAW LKGDHRIRPS RSSQSAMLRS LVPR.
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 :
OTOR Human, HisDescription:
Otoraplin Human Recombinant, His Tag
Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.
Product # :
CYT-884Price :
Quantity :
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Shipped with Ice Packs
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Description
OTOR Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-128 a.a) and having a molecular mass of 14.3kDa. OTOR is fused to a 25 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
OTOR protein solution (0.25mg/ml) containing Phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
OTOR proteins is also known as fibrocyte-derived protein (Fdp) and Melanoma inhibitory activity-like (MIAL). Otoraplin is a member of the melanoma-inhibiting activity gene family. Otoraplin is a secreted 16 kDa globular protein that is expressed in the inner ear by periotic mesenchyme and developing and mature fibrocytes. OTOR is highly homologous to MIA/cartilage-derived retinoic acid-sensitive protein (CD-RAP), which is a cartilage-specific protein that is also expressed in malignant melanoma cells. The 111 amino acid mature human otoraplin contains 1 SH3 domain (46 – 107 amino acids) and a Tyr at position 50 that is reportedly sulfated. Otoraplin takes pasrt in the initiation of periotic mesenchyme chondrogenesis.
Otoraplin is secreted through the Golgi apparatus and plays a role in cartilage development and maintenance. A frequent polymorphism in the translation start codon of OTOR can abolish translation and may be associated with forms of deafness. -
Synonyms
Otoraplin, Melanoma Inhibitory Activity-Like Protein, Fibrocyte-Derived Protein, FDP, MIAL1, MIAL, Melanoma inhibitory activity-like protein.
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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 MGSHMLASKK LCADDECVYT ISLASAQEDY NAPDCRFINV KKGQQIYVYS KLVKENGAGE FWAGSVYGDG QDEMGVVGYF PRNLVKEQRV YQEATKEVPT TDIDFFCE.
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 :
TIPIN HumanDescription:
TIMELESS Interacting Protein Human Recombinant
TIMELESS Interacting Protein, CSM3 Homolog.
Product # :
PRO-1710Price :
Quantity :
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Shipped with Ice Packs
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Description
TIPIN Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 324 amino acids (1-301) and having a molecular mass of 36.9kDa.TIPIN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The TIPIN solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 0.15M NaCl, 1mM DTT and 10% glycerol.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
TIPIN is a member of the CSM3 family. TIPIN protein is essential for normal advancement of S-phase and vital for cell existence after DNA damage or replication stress. TIPIN is specifically necessary for the ATR - CHEK1 pathway in the replication checkpoint induced by ultraviolet light.
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Synonyms
TIMELESS Interacting Protein, CSM3 Homolog.
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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 MGSMLEPQEN GVIDLPDYEH VEDETFPPFP PPASPERQDG EGTEPDEESG NGAPVPVPPK RTVKRNIPKL DAQRLISERG LPALRHVFDK AKFKGKGHEA EDLKMLIRHM EHWAHRLFPK LQFEDFIDRV EYLGSKKEVQ TCLKRIRLDL PILHEDFVSN NDEVAENNEH DVTSTELDPF LTNLSESEMF ASELSRSLTE EQQQRIERNK QLALERRQAK LLSNSQTLGN DMLMNTPRAH TVEEVNTDED QKEESNGLNE DILDNPCNDA IANTLNEEET LLDQSFKNVQ QQLDATSRNI TEAR
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 :
FSTL1 Human, HEKDescription:
Follistatin Like 1 Human Recombinant, HEK
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
Product # :
CYT-1027Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
FSTL1 Human Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (a.a 21-308) containing 296 amino acids including a 8 a.a C-terminal His tag. The total molecular mass is 33.8kDa (calculated).
Source
HEK293 cells.
Formulation
FSTL1 filtered (0.4 µm) and lyophilized from 0.5mg/ml in phosphate buffered saline and 5 % (w/v) trehalose, pH 7.4.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
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Introduction
FSTL1 protein resembles follistatin, an activin-binding protein. FSTL1 is an autoantigen associated with rheumatoid arthritis and it holds an FS section, a follistatin-like sequence having 10 conserved cysteine residues.
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Synonyms
Follistatin-related protein 1, Follistatin-like protein 1, FSTL1, FRP, Follistatin Like 1, FSL1, MIR198.
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Physical Appearance
Filtered White lyophilized (freeze-dried) powder.
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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 one week at 4°C.
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Solubility
It is recommended to add deionized water to prepare a working stock solution of approximately 0.5mg/ml and let the lyophilized pellet dissolve completely. FSTL1 is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.
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Amino Acid Sequence
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
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Background
What is the molecular weight/Mw of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein has a total Mw of 33.8kDa.
What is the source or expression system of FSTL1 HUMAN, HEK Protein?
HEK293 cells.
What is the Purity of FSTL1 HUMAN, HEK Protein?
FSTL1 HUMAN, HEK Protein is >95% pure as determined by SDS-PAGE.
What is the Biological Activity of FSTL1 HUMAN, HEK Protein?
The biological functionality of FSTL1 HUMAN, HEK Protein will be determined in the future.
What is the amino acid sequence of FSTL1 HUMAN, HEK Protein?
EEELRSKSKI CANVFCGAGR ECAVTEKGEP TCLCIEQCKP HKRPVCGSNG KTYLNHCELH RDACLTGSKI QVDYDGHCKE KKSVSPSASP VVCYQSNRDE LRRRIIQWLE AEIIPDGWFS KGSNYSEILD KYFKNFDNGD SRLDSSEFLK FVEQNETAIN ITTYPDQENN KLLRGLCVDA LIELSDENAD WKLSFQEFLK CLNPSFNPPE KKCALEDETY ADGAETEVDC NRCVCACGNW VCTAMTCDGK NQKGAQTQTE EEMTRYVQEL QKHQETAEKT KRVSTKEIHH HHHHHH.
What applications can FSTL1 HUMAN, HEK Protein be used in?
FSTL1 HUMAN, HEK Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for FSTL1 HUMAN, HEK Protein?
The endotoxin level is minimal, FSTL1 HUMAN, HEK 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.
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Name :
HAUS1 HumanDescription:
HAUS Augmin-Like Complex, Subunit 1 Human Recombinant
HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.
Product # :
PRO-1077Price :
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Description
HAUS1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 302 amino acids (1-278 a.a) and having a molecular mass of 34.4kDa.HAUS1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
HAUS1 protein solution (0.25mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 50% glycerol, 0.2M NaCl and 2mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
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Introduction
HAUS augmin-like complex subunit 1 (HAUS1) is 1 of 8 subunits of the 390kDa human augmin complex/ HAUS complex. The augmin complex is a microtubule-binding complex required in microtubule generation within the mitotic spindle and is imperative to mitotic spindle compilation. HAUS1 contributes to mitotic spindle assembly, maintenance of centrosome integrity and completion of cytokinesis as part of the HAUS augmin-like complex. HAUS1 is broadly expressed, especially in the pancreas, kidney, skeletal muscle, liver and heart. However it is weakly expressed in the lung, brain and placenta. HAUS1-depleted cells hold functional cell cycle checkpoints, but the depletion reduces the G2/M cell cycle compartment and stimulates apoptosis. The HAUS1 protein level remains constant through the cell cycle.
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Synonyms
HAUS augmin-like complex subunit 1, Coiled-coil domain-containing protein 5, Enhancer of invasion-cluster, HEI-C, HAUS1, CCDC5, HEIC, HsT1461.
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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 MGSHMEPQEE RETQVAAWLK KIFGDHPIPQ YEVNPRTTEI LHHLSERNRV RDRDVYLVIE DLKQKASEYE SEAKYLQDLL MESVNFSPAN LSSTGSRYLN ALVDSAVALE TKDTSLASFI PAVNDLTSDL FRTKSKSEEI KIELEKLEKN LTATLVLEKC
LQEDVKKAEL HLSTERAKVD NRRQNMDFLK AKSEEFRFGI KAAEEQLSAR GMDASLSHQS LVALSEKLAR LKQQTIPLKK KLESYLDLMP NPSLAQVKIE EAKRELDSIE AELTRRVDMM 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 :
SCF CanineDescription:
Stem Cell Factor Canine Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-194Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem Cell Factor Canine Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18.4kDa Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a 0.2µm filtered concentrated solution in PBS, pH 7.4.
Purity
Greater than 97.0% as determined by HPLC and SDS-PAGE.
Biological Activity
Fully biologically active when compared to standard. The ED50 as calculated by the dose-dependent stimulation of the proliferation of human TF-1 cells is less than 2.0ng/ml, corresponding to a specific activity of 5,000,000IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases. SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid).
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Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SCF although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
KGICGKRVTD DVKDVTKLVA NLPKDYKIAL KYVPGMDVLP SHCWISVMVE QLSVSLTDLL DKFSNISEGL SNYSIIDKLV KIVDDLVECT EGYSFENVKK APKSPELRLF TPEEFFRIFN RSIDAFKDLE TVASKSSECV VSSTLSPDKD SRVSVTKPFM LPPVA
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.
- View Data Sheet
Name :
SDF 1a MouseDescription:
Stromal Cell-Derived Factor-1 Alpha Mouse Recombinant (CXCL12)
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
Product # :
CHM-324Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
- formulation
- purity
- biological activity
- More Info
Description
Stromal Cell-Derived Factor-1 alpha Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 68 amino acids and having a molecular mass of 8 kDa. The SDF-1a is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was Lyophilized from a sterile filtered aqueous solution containing 0.1% Trifluoroacetic Acid (TFA).
Purity
Greater than 95% as determined by SDS-PAGE.
Biological Activity
The specific activity as determined by its ability to chemoattract human peripheral blood monocytes at 50-100 ng/ml corresponding to a Specific Activity of 10,000-20,000IU/mg.
More Info
-
Introduction
SDF-1 (stromal cell-derived factor-1) is small cytokine belonging to the chemokine family that is officially designated Chemokine (C-X-C motif) ligand 12 (CXCL12). It is produced in two forms, SDF-1?/CXCL12a and SDF-1?/CXCL12b, by alternate splicing of the same gene. Chemokines are characterized by the presence of four conserved cysteines, which form two disulfide bonds. The CXCL12 proteins belong to the group of CXC chemokines, whose initial pair of cysteines are separated by one intervening amino acid. CXCL12 is strongly chemotactic for lymphocytes and has been implicated as an important cell co-ordinator during development. During embryogenesis it directs the migration of hematopoietic cells from foetal liver to bone marrow. Mice which were knocked-out for CXCL12 gene were lethal before the birth or within just 1 hour of life. As another role, CXCL12a alters also the electrophysiology of neurons. CXCL12 was shown to be expressend in many tissues in mice (including brain, thymus, heart, lung, liver, kidney, spleen and bone marrow).
The receptor for this chemokine is CXCR4, which was previously called fusin. This CXCL12-CXCR4 interaction used to be considered exclusive (unlike for other chemokines and their receptors), but recently it was suggested that CXCL12 is also bound by CXCR7 receptor.
The gene for CXCL12 is located on human chromosome 10. In human and mouse both CXCL12 and CXCR4 show high identity of sequence: 99% and 90%, respectively. -
Synonyms
SDF-1, CXCL12, Pre-B cell growth-stimulating factor, PBSF, hIRH, chemokine (C-X-C motif) ligand 12, SDF1, SDF1A, TPAR1, SCYB12, SDF-1a, TLSF-a, 12-O-tetradecanoylphorbol 13-acetate repressed protein 1, Thymic lymphoma cell-stimulating factor, TLSF.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized SDF-1a although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CXCL12 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 Stromal Cell-Derived Factor-1a in sterile 18MΩ-cm H2O 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 Lys-Pro-Val-Ser-Leu.
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.
- View Data Sheet
Name :
NPM1 HumanDescription:
Nucleophosmin Human Recombinant
Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.
Product # :
PRO-1120Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
NPM1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 314 amino acids (1-294 a.a) and having a molecular mass of 34.7kDa.NPM1 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
NPM1 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 10% glycerol, 0.15M NaCl and 1mM DTT.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Nucleophosmin (NPM1) is a phosphoprotein which shuffles between the nucleus and the cytoplasm. NPM1 is assumed to be involved in a number of processes including regulation of the ARF/p53 pathway. Several genes fusion partners have been described, particularly the anaplastic lymphoma kinase gene on chromosome 2. NPM1 gene mutations are linked with acute myeloid leukemia.
-
Synonyms
Nucleophosmin, NPM, Nucleolar phosphoprotein B23, Nucleolar protein NO38, Numatrin, NPM1, NPM, B23.
-
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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MEDSMDMDMS PLRPQNYLFG CELKADKDYH FKVDNDENEH QLSLRTVSLG AGAKDELHIV EAEAMNYEGS PIKVTLATLK MSVQPTVSLG GFEITPPVVL RLKCGSGPVH ISGQHLVAVE EDAESEDEEE EDVKLLSISG KRSAPGGGSK VPQKKVKLAA
DEDDDDDDEE DDDEDDDDDD FDDEEAEEKA PVKKSIRDTP AKNAQKSNQN GKDSKPSSTP RSKGQESFKK QEKTPKTPKG PSSVEDIKAK MQASIEKGGS LPKVEAKFIN YVKNCFRMTD QEAIQDLWQW RKSL.
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.
- View Data Sheet
Name :
S100A9 HumanDescription:
S100 Calcium Binding Protein A9 Human Recombinant
Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.
Product # :
PRO-814Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
S100A9 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 122 amino acids (1-114 a.a.) and having a molecular mass of 14.3kDa. S100A9 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
S100A9 Human solution containing 20mM Tris HCl pH-8, 0.1M NaCl and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
S100A9 is part of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100A9 protein is localized in the cytoplasm and/or nucleus of a wide range of cells, and participates in the regulation of several cellular processes such as cell cycle progression and differentiation. S100 genes include no less than 13 proteins which are localized as a cluster on chromosome 1q21. S100A9 is involved in the inhibition of casein kinase and altered expression of this protein is associated with the disease cystic fibrosis.
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Synonyms
Calgranulin B, 60B8AG, CAGB, CFAG, CGLB, L1AG, LIAG, MAC387, MIF, MRP14, NIF, P14, Protein S100-A9, S100 calcium-binding protein A9.
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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.
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Amino Acid Sequence
MTCKMSQLER NIETIINTFH QYSVKLGHPD TLNQGEFKEL VRKDLQNFLK KENKNEKVIE HIMEDLDTNA DKQLSFEEFI MLMARLTWAS HEKMHEGDEG PGHHHKPGLG EGTPLEHHHH HH.
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.
- View Data Sheet
Name :
SCF Human, Sf9Description:
Stem Cell Factor Human Recombinant, Sf9
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
Product # :
CYT-421Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem Cell Factor Human Recombinant produced in insect cells is a single, glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18409 Dalton. The SCF is fused to a C-terminal His-tag (6xHis) and purified by proprietary chromatographic techniques.
Source
Sf9, Insect Cells.
Formulation
The protein is supplied in 1xPBS, pH 7.4.
Purity
Greater than 98.0% as determined by analysis by SDS-PAGE.
Biological Activity
The ED50 as determined by the dose-dependent stimulation of Human TF-1 cells is typically 1-5 ng/ml.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid). -
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor in 10mM acetic acid not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor as a Reference Standard.
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.
- View Data Sheet
Name :
Lymphotactin Human, HisDescription:
Lymphotactin Human Recombinant (XCL1), His Tag
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
Product # :
CHM-357Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
XCL1 Human Recombinant produced in E.Coli is a single,non-glycosylated, polypeptide chain containing 114 amino acids (22-114 a.a.) and having a molecular mass of 12.5 kDa. The XCL1 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Recombinant XCL1 contains 20mM Tris buffer pH-8, 200mM NaCl, 2mM DTT and 30% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
XCL1 is a small cytokine belonging to the XC chemokine family that is also known as lymphotactin. It is located in high levels in spleen, thymus, intestine and peripheral blood leukocytes, and at lower levels in lung, prostate gland and ovary. Cellular sources for XCL1 include activated thymic and peripheral blood CD8+ T cells. This chemokine attracts T cells. In humans, XCL1 is closely related to another chemokine called XCL2, whose gene is found at the same locus on chromosome 1. XCL1 induces it chemotactic function by binding to a chemokine receptor called XCR1.
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Synonyms
XCL1, Cytokine SCM-1, ATAC, Lymphotaxin, SCM-1-alpha, Small inducible cytokine C1, XC chemokine ligand 1, LTN, LPTN, SCM1, SCM-1, SCYC1, SCM-1a.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG.
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.
- View Data Sheet
Name :
SQSTM1 HumanDescription:
Sequestosome 1 Human Recombinant
A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.
Product # :
PRO-806Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
SQSTM1 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 364 amino acids (1-356 a.a.) and having a molecular mass of 39.7 kDa. SQSTM1 protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography.
Source
Escherichia Coli.
Formulation
SQSTM1 Human 0.5mg/ml solution containing 20mM Tris-HCl pH-8, 1mM DTT and 10% glycerol.
Purity
Greater than 85% as determined by SDS-PAGE.
More Info
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Introduction
SQSTM1 is an adapter protein which binds ubiquitin and mediates the activation of NFKB1 by TNF-a, NGF and IL-1. SQSTM1 is involved in titin/TTN downstream signaling in muscle cells. SQSTM1 controls signaling cascades through ubiquitination. SQSTM1 participates in cell differentiation, apoptosis, immune response and regulation of K(+) channels. Mutations in UBA domain of the SQSTM1 protein cause Paget’s disease because the UBA is essential for aggregate sequestration and cell survival.
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Synonyms
A170, OSIL, p60, p62, p62B, PDB3, ZIP3, EBIAP, ORCA, OSIL, SQSTM1.
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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.
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Amino Acid Sequence
MAMSYVKDDI FRIYIKEKKE CRRDHRPPCA QEAPRNMVHP NVICDGCNGP VVGTRYKCSV CPDYDLCSVC EGKGLHRGHT KLAFPSPFGH LSEGFSHSRW LRKVKHGHFG WPGWEMGPPG NWSPRPPRAG EARPGPTAES ASGPSEDPSV NFLKNVGESV AAALSPLGIE VDIDVEHGGK RSRLTPVSPE SSSTEEKSSS QPSSCCSDPS KPGGNVEGAT QSLAEQMRKI ALESEGRPEE QMESDNCSGG DDDWTHLSSK EVDPSTGELQ SLQMPESEGP SSLDPSQEGP TGLKEAALYP HLPPEADPRL IESLSQMLSM GFSDEGGWLT RLLQTKNYDI GAALDTIQYS KHPPPLLEHH 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.
- View Data Sheet
Name :
Thymosin a1 humanDescription:
Thymosin a1 Acetate
Product # :
HOR-243Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Thymosin a1 acetate, also known as thymalfasin has immunoregulatory properties enhancing immune functions. Thymosin a1 has a molecular formula of C129H215N33O55 a.a. sequence of Ac-Ser-Asp-Ala-Ala-Val-Asp-Thr-Ser-Ser-Glu-Ile-Thr-Thr-Lys-Asp-Leu-Lys-Glu-Lys-Lys-Glu-Val-Val-Glu-Glu-Ala-Glu-Asn-OH and having a Mw of 3108.32 Dalton.
Formulation
The protein (1mg/ml) was lyophilized with no additives.
Purity
Greater than 99.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
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Introduction
Thymalfasin is a synthetic analogue of thymosin-alpha-1, a 28-amino acid protein derived from the precursor protein prothymosin-alpha. Exhibiting a variety of immunoregulating properties, thymosin-alpha-1 induces differentiation of murine T-cell precursors and human thymocytes and the terminal differentiation of functionally immature cord blood lymphocytes and induces production of IL-2, high affinity IL-2 receptors, and B-cell growth factors by peripheral blood mononuclear cells. T-helper and cytotoxic/suppressor T-cell populations are targets of thymosin activity. Thymosin-alpha-1 has been shown to increase the efficiency of antigen presentation by macrophages and to be an endogenous modulator of alpha-thrombin activity.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized Thymosin a1 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thymalfasin 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 Thymosin a1 in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
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Background
What is the molecular weight/Mw of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein has a total Mw of 3.1kDa.
What is the Purity of THYMOSIN-A1 HUMAN Protein?
THYMOSIN-A1 HUMAN Protein is >99% pure as determined by SDS-PAGE.
What is the Biological Activity of THYMOSIN-A1 HUMAN Protein?
The biological functionality of THYMOSIN-A1 HUMAN Protein will be determined in the future.
What applications can THYMOSIN-A1 HUMAN Protein be used in?
THYMOSIN-A1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for THYMOSIN-A1 HUMAN Protein?
The endotoxin level is minimal, THYMOSIN-A1 HUMAN Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
OSM HumanDescription:
Oncostatin-M Human Recombinant
OSM, MGC20461.
Product # :
CYT-231Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
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- source
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Description
Oncostatin-M Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids and having a molecular mass of 26kDa. The OSM is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution containing PBS pH-7.4.
Purity
Greater than 95.0% as determined by
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cells is < 2 ng/ml, corresponding to a Specific Activity of 500,000IU/mg.More Info
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Introduction
Oncostatin M is a member of a cytokine family that includes leukemia-inhibitory factor, granulocyte colony-stimulating factor, and interleukin 6. This gene encodes a growth regulator which inhibits the proliferation of a number of tumor cell lines. It regulates cytokine production, including IL-6, G-CSF and GM-CSF from endothelial cells.
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Synonyms
OSM, MGC20461.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Oncostatin M although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Oncostatin 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 Oncostatin M in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
AAIGSCSKEY RVLLGQLQKQ TDLMQDTSRL LDPYIRIQGL DVPKLREHCR
ERPGAFPSEE TLRGLGRRGF LQTLNATLGC VLHRLADLEQ RLPKAQDLER
SGLNIEDLEK LQMARPNILG LRNNIYCMAQ LLDNSDTAEP TKAGRGASQP
PTPTPASDAF QRKLEGCRFL HGYHRFMHSV GRVFSKWGES PNRSRRHSPH
QALRKGVRRT RPSRKGKRLM TRGQLPR. -
Protein content
Protein quantitation was carried out by two independent methods1. UV spectroscopy at 280 nm using the absorbency value of 0.45 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using standard solution of Oncostatin as Reference.
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.
- View Data Sheet
Name :
MINA HumanDescription:
MYC Induced Nuclear Antigen Human Recombinant
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
Product # :
PRO-2078Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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Description
MINA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465 a.a) and having a molecular mass of 54.9kDa. MINA is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MINA protein solution (0.25mg/ml) containing 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
MYC Induced Nuclear Antigen, also known as MINA is an oxygenase which can function both as a histone lysine demethylase and a ribosomal histidine hydroxylase. MINA is involved in the demethylation of trimethylated Lys-9 on histone H3 (H3K9me3), leading to an increase in ribosomal RNA expression. MINA also catalyzes the hydroxylation of 60S ribosomal protein L27a on His-39. In addition, MINA plays a significant role in cell growth and survival. MINA is implicated in ribosome biogenesis, probably in the duration of the assembly process of pre-ribosomal particles.
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Synonyms
MYC Induced Nuclear Antigen, MINA53, MDIG, 60S Ribosomal Protein L27a Histidine Hydroxylase, Mineral Dust-Induced Gene Protein, Histone Lysine Demethylase MINA Ribosomal Oxygenase MINA, Nucleolar Protein 52, NO52, ROX, Bifunctional Lysine-Specific Demethylase And Histidyl-Hydroxylase MINA, Myc-Induced Nuclear Antigen, 53 KDa, Mineral Dust Induced Gene Protein, MYC-Induced Nuclear Antigen, EC 1.14.11.-, Bifunctional lysine-specific demethylase and histidyl-hydroxylase MINA.
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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.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MPKKAKPTGS GKEEGPAPCK QMKLEAAGGP SALNFDSPSS LFESLISPIK TETFFKEFWE QKPLLIQRDD PALATYYGSL FKLTDLKSLC SRGMYYGRDV NVCRCVNGKK KVLNKDGKAH FLQLRKDFDQ KRATIQFHQP QRFKDELWRI QEKLECYFGS LVGSNVYITP AGSQGLPPHY DDVEVFILQL EGEKHWRLYH PTVPLAREYS VEAEERIGRP VHEFMLKPGD LLYFPRGTIH QADTPAGLAH STHVTISTYQ NNSWGDFLLD TISGLVFDTA KEDVELRTGI PRQLLLQVES TTVATRRLSG FLRTLADRLE GTKELLSSDM KKDFIMHRLP PYSAGDGAEL STPGGKLPRL DSVVRLQFKD HIVLTVLPDQ DQSDETQEKM VYIYHSLKNS RETHMMGNEE ETEFHGLRFP LSHLDALKQI WNSPAISVKD LKLTTDEEKE SLVLSLWTEC LIQVV.
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.
- View Data Sheet
Name :
SCF MouseDescription:
Stem Cell Factor Mouse Recombinant
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.
Product # :
CYT-275Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
Stem Cell Factor Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 165 amino acids and having a molecular mass of 18309 Dalton. The SCF is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated (1mg/ml) solution in water containing 0.02% NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by SEC-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by the dose-dependant stimulation of Human TF-1 cell line is < 10 ng/ml, corresponding to a Specific Activity of 1x105 IU/mg.More Info
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Introduction
Stem cell factor / KIT ligand (SCF) is a cytokine which binds CD117(c-Kit). SCF is also known as "steel factor" or "c-kit ligand". SCF exists in two forms, cell surface bound SCF and soluble (or free) SCF. Soluble SCF is produced by the cleavage of surface bound SCF by metalloproteases.
SCF is a growth factor important for the survival, proliferation, and differentiation of hematopoietic stem cells and other hematopoietic progenitor cells. One of its roles is to change the BFU-E (burst-forming unit-erythroid) cells, which are the earliest erythrocyte precursors in the erythrocytic series, into the CFU-E (colony-forming unit-erythroid). -
Synonyms
Kit ligand Precursor, C-kit ligand, SCF, Mast cell growth factor, MGF, SF, KL-1, Kitl, DKFZp686F2250, Hematopoietic growth factor KL, Steel factor.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized KIT ligand although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution SCF 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 Stem Cell Factor in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Amino Acid Sequence
MKEICGNPVT DNVKDITKLV ANLPNDYMIT LNYVAGMDVL PSHCWLRDMV IQLSLSLTTL LDKFSNISEG LSNYSIIDKL GKIVDDLVLC MEENAPKNIK ESPKRPETRS FTPEEFFSIF NRSIDAFKDF MVASDTSDCV LSSTLGPEKD SRVSVTKPFM LPPVA.
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Protein content
Protein quantitation was carried out by two independent methods:1. UV spectroscopy at 280 nm using the absorbency value of 0.52 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). 2. Analysis by RP-HPLC, using a standard solution of Stem Cell Factor as a Reference Standard.
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 :
MYOZ1 HumanDescription:
Myozenin 1 Human Recombinant
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
Product # :
PRO-1652Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
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Description
MYOZ1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 322 amino acids (1-299 a.a.) and having a molecular mass of 34.1kDa.MYOZ1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
MYOZ1 protein solution (1mg/ml) contains 20mM Tris-HCl buffer, (pH 8.0), 0.4M UREA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
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Introduction
Myozenin 1 (MYOZ1) is a member of the myozenin family. MYOZ1 is mostly expressed in the skeletal muscle. Members of the myozenin family act as calcineurin-interacting proteins which helps tether calcineurin to the sarcomere of cardiac and skeletal muscle. The myozenin family plays a significant role in modulation of calcineurin signaling.
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Synonyms
CS-2, FATZ, MYOZ, Calsarcin-2, Filamin-, actinin- and telethonin-binding protein,Protein FATZ, MYOZ1.
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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 MGSMPLSGTP APNKKRKSSK LIMELTGGGQ ESSGLNLGKK ISVPRDVMLE ELSLLTNRGS KMFKLRQMRV EKFIYENHPD VFSDSSMDHF QKFLPTVGGQ LGTAGQGFSY SKSNGRGGSQ AGGSGSAGQY GSDQQHHLGS GSGAGGTGGP AGQAGRGGAA GTAGVGETGS GDQAGGEGKH ITVFKTYISP WERAMGVDPQ QKMELGIDLL AYGAKAELPK YKSFNRTAMP YGGYEKASKR MTFQMPKFDL GPLLSEPLVL YNQNLSNRPS FNRTPIPWLS SGEPVDYNVD IGIPLDGETE 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 :
SUGT1 HumanDescription:
SGT1 Recombinant Human
SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae), SGT1, Putative 40-6-3 protein, SGT1B protein.
Product # :
PRO-096Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
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- description
- source
- formulation
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Description
SGT1 produced in E.Coli is a single, non-glycosylated polypeptide chain containing 252 amino acids (115-365.a.a) and having a molecular mass of 30.7kDa. SGT1 is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The SGT1 protein solution (0.5mg/1ml) is formulated in 20 mM Tris-HCl buffer (pH8.0), 0.1M NaCl, 1mM DTT and 20% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Introduction
SUGT1 is homolog to yeast protein SGT1, a regulator of the cell cycle which is vital for G1/S and G2/M transitions. SUGT1 holds a CS domain, a SGS domain, a p23 domain and three tetratricopeptide repeats (TPR). SUGT1 protein associates with Skp1 p19 and CUL-1, subunits of the SCF ubiquitin ligase complex, and is believed to take a part in protein degradation. Furthermore, SUGT1 is essential for the kinetochores assembly, and has a role as a co-chaperone for HSP90.
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Synonyms
SGT1, suppressor of G2 allele of SKP1 (S. cerevisiae), SGT1, Putative 40-6-3 protein, SGT1B protein.
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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.Please avoid freeze thaw cycles.
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Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MHRVGQAGLQ LLTSSDPPAL DSQSAGITGA DANFSVWIKR CQEAQNGSES EVWTHQSKIK YDWYQTESQVVITLMIKNVQ KNDVNVEFSE KELSALVKLP SGEDYNLKLE LLHPIIPEQS TFKVLSTKIE IKLKKPEAVR WEKLEGQGDV PTPKQFVADVKNLYPSSSPY TRNWDKLVGE IKEEEKNEKL EGDAALNRLF QQIYSDGSDE VKRAMNKSFM ESGGTVLSTN WSDVGKRKVE INPPDDMEWKKY
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 :
s100bb BovineDescription:
s100bb Bovine homodimer
Product # :
PRO-2796Price :
Quantity :
Shipping Method :
Shipped at Room temp
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- source
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Description
s100bb Bovine is suitable for use as a standard in immunoassay and as an immunogen for antiserum production.
Source
Bovine brain tissue.
Formulation
s100bb was lyophilized from 5mM Tris-HCl, pH 7.5, 2mM EDTA and 5mM 2-mercaptoethanol.
Purity
Greater than 95.0% .
More Info
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized s100bb homodimer although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution s100bb 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 s100bb in sterile 18MΩ-cm H2O containing 5mM 2- mercaptoethanol not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
S100BB, a member of the S100 family of proteins, is a calcium-binding protein that plays a significant role in various cellular processes, particularly in the central nervous system (CNS). Initially identified as a brain-specific protein, S100BB has captured the attention of researchers due to its involvement in neurological signaling, brain development, and its potential implications in neurological disorders. This research delves into the enigmatic world of S100BB, aiming to uncover its diverse functions, regulatory mechanisms, and its relevance in health and disease.
Discovery and Structural Insights:
S100BB was first discovered in the brain, primarily localized in astrocytes, a type of glial cell in the CNS. Structurally, S100BB is characterized by its EF-hand motifs, allowing it to bind calcium ions, a property crucial for its function. These calcium-binding abilities enable S100BB to participate in intricate cellular signaling pathways, making it a vital player in the dynamic communication within the CNS.
Neurological Signaling and Plasticity:
Within the CNS, S100BB has been implicated in neuronal signaling and synaptic plasticity. It interacts with several target proteins, modulating their activities and influencing processes like neurotransmitter release and neuronal differentiation. Furthermore, S100BB participates in the regulation of intracellular calcium levels, a key factor in neuronal excitability and synaptic transmission. Understanding these roles is vital for unraveling the complexities of neurological function and plasticity.
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 :
TSH CanineDescription:
Thyroid Stimulating Hormone Canine Recombinant
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
Product # :
HOR-049Price :
Quantity :
Shipping Method :
Shipped at Room temp
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Description
TSH Canine is a heterodimeric glycoprotein consisting of 2 non-covalently linked subunits, an alpha subunit (96 a.a) and a beta subunit (118 a.a). TSH Canine is produced by co-expression of the alpha and beta subunits of TSH. Beta subunit contains alanine instead of valine at position 81.
Source
Mammalian cell line.
Formulation
TSH was lyophilized from 150mM NaCl, 10mM K-phosphate, pH 7.4, 0.1% CHAPS and 100mM D-mannitol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
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Synonyms
Glycoprotein hormones alpha chain, Anterior pituitary glycoprotein hormones common subunit alpha, Follitropin alpha chain, Follicle-stimulating hormone alpha chain, FSH-alpha, Lutropin alpha chain, Luteinizing hormone alpha chain, LSH-alpha, Thyrotropin alpha chain, Thyroid-stimulating hormone alpha chain, TSH-alpha, Choriogonadotropin alpha chain, Chorionic gonadotrophin alpha subunit, CG-alpha, Thyrotropin subunit beta, Thyroid-stimulating hormone subunit beta, TSH-beta, TSH-B, Thyrotropin beta chain, Thyrotropin alfa.
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Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
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Stability
Lyophilized TSH although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Thyroid Stimulating Hormone 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 TSH in deionized H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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Background
Thyroid Stimulating Hormone (TSH), a pivotal glycoprotein hormone secreted by the anterior pituitary gland, stands as the master regulator of thyroid function. Its intricate control over thyroid hormone synthesis and secretion makes it a linchpin in the delicate balance of the endocrine system. The study of TSH, particularly in the form of TSH Recombinant Protein, has not only provided profound insights into thyroid physiology but has also revolutionized diagnostic methods, therapeutic interventions, and our understanding of various thyroid disorders. This research delves into the multifaceted realm of TSH, exploring its structural intricacies, physiological roles, and its far-reaching implications in both clinical and research settings.
Structural Insights into TSH:
TSH, a heterodimeric protein consisting of alpha and beta subunits, possesses a distinctive structure crucial for its biological activity. The beta subunit contains a unique hinge region, allowing flexibility in its interactions with the thyroid follicular cells. Understanding these structural nuances is fundamental for comprehending TSH's receptor binding, signaling cascades, and its intricate feedback mechanisms governing thyroid hormone production.
Physiological Significance in Thyroid Regulation:
TSH orchestrates thyroid function by binding to its specific receptors on the thyroid gland, stimulating iodine uptake, thyroid hormone synthesis, and secretion. This process is indispensable for maintaining the body's metabolism, energy balance, and overall growth and development. TSH's meticulous control over thyroid activity ensures the precise release of thyroid hormones, essential for numerous physiological processes and maintaining homeostasis.
Diagnostic and Therapeutic Applications:
In the realm of diagnostics, TSH assays utilizing TSH Recombinant Protein have revolutionized the detection and monitoring of thyroid disorders, particularly hypothyroidism and hyperthyroidism. By measuring TSH levels, clinicians can assess thyroid function, enabling early diagnosis and personalized treatment strategies. Moreover, recombinant TSH finds applications in diagnostic imaging, enhancing the accuracy of radioiodine scans for thyroid cancer diagnosis and treatment.
Innovative Therapies and Future Prospects:
Recombinant TSH has paved the way for innovative therapeutic interventions, particularly in the management of thyroid cancer. Thyroid remnant ablation, a crucial step in thyroid cancer treatment, involves the administration of radioiodine following recombinant TSH stimulation, maximizing the therapeutic efficacy while minimizing the radiation exposure to surrounding tissues. Ongoing research explores the potential of TSH receptor agonists and antagonists, offering new avenues for targeted therapies in thyroid-related disorders.
TSH Recombinant Protein, with its profound influence on thyroid function and its applications in diagnostics and therapeutics, stands at the forefront of endocrine research. Its intricate roles in thyroid regulation, metabolism, and growth highlight its significance in human physiology. As our understanding of TSH deepens, it not only aids in the development of innovative treatments but also opens new avenues for exploring the complex interplay between hormones, receptors, and physiological responses. This research not only illuminates the vital role of TSH but also underscores its potential in shaping the future of thyroid-related healthcare.
What is the source or expression system of TSH CANINE Protein?
Mammalian cell line.
What is the Purity of TSH CANINE Protein?
TSH CANINE Protein is >90% pure as determined by SDS-PAGE.
What is the Biological Activity of TSH CANINE Protein?
The biological functionality of TSH CANINE Protein will be determined in the future.
What applications can TSH CANINE Protein be used in?
TSH CANINE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for TSH CANINE Protein?
The endotoxin level is minimal, TSH CANINE 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.