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Search results

1000 results found for “Gluteradoxin”

Name

Description

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  • View Data Sheet

    Name :

    DsbC

    Description:

    Disulfide-Bond Isomerase Recombinant

    Disulfide-bond isomerase C, dsbC, xprA, Disulfide-bond isomerase (DsbC) E.Coli, Thiol:disulfide interchange protein dsbC, Disulfide-bond isomerase C Thiol:disulfide interchange protein dsbC .

    Product # :

    ENZ-291

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    Description

    Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 217 amino acids (21-236) and having a molecular mass of 23.6 kDa.DsbC is purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    1 mg/ml solution containing 20mM Tris-HCl buffer pH 7.5 and 2mM EDTA.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. DsbC is periplasmic enzyme known as a disulfide isomerase and can convert aberrant disulfide bonds to correct ones.

    • Synonyms

      Disulfide-bond isomerase C, dsbC, xprA, Disulfide-bond isomerase (DsbC) E.Coli, Thiol:disulfide interchange protein dsbC, Disulfide-bond isomerase C Thiol:disulfide interchange protein dsbC .

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MDDAAIQQTL AKMGIKSSDI QPAPVAGMKT VLTNSGVLYI TDDGKHIIQG PMYDVSGTAP VNVTNKMLLK QLNALEKEMI VYKAPQEKHV ITVFTDITCG YCHKLHEQMA DYNALGITVR YLAFPRQGLD SDAEKEMKAI WCAKDKNKAF DDVMAGKSVA PASCDVDIAD HYALGVQLGV SGTPAVVLSN GTLVPGYQPP KEMKEFLDEH QKMTSGK.

    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.

    Disulfide Bond Isomerase
  • View Data Sheet

    Name :

    SNAPIN Human

    Description:

    SNAP Associated Protein Human Recombinant

    SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    Product # :

    PRO-663

    Price :

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    Description

    SNAPIN Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 156 amino acids (1-136) and having a molecular mass of 17 kDa. SNAPIN is fused to 20 amino acid His Tag at N-terminus and purified by standard chromatography techniques.

    Source

    Escherichia Coli.

    Formulation

    The protein solution contains 20mM Tris-HCl pH-8, 5mM DTT, 2mM EDTA, 0.2M NaCl, and 40% glycerol.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SNAPIN is involved in the neurotransmitter release process through its modulation of the sequential interactions between the SNAREs and synaptotagmin. SNAPIN is part of the SNARE complex of proteins that is needed for synaptic vesicle docking and fusion. SNAPAP is enriched in neurons and exclusively located on synaptic vesicle membrane protein. SNAPIN is also an important factor of the BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules.

    • Synonyms

      SNAPAP, SNARE-associated protein Snapin, Synaptosomal-associated protein 25-binding protein, SNAP-associated protein, SNAPIN, SNAP25BP.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINEDQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK.

    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.

    Snapin Human
  • View Data Sheet

    Name :

    CALB2 Human

    Description:

    Calbindin-2 Human Recombinant

    Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    Product # :

    PRO-401

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    Description

    CALB2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 291 amino acids (1-271 a.a.) and having a molecular mass of 33.7kDa.The CALB2 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The CALB2 1mg/ml protein solution contains 20mM Tris-HCl buffer pH-8 & 10% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

    • Synonyms

      Calretinin, CR, CALB2, CAB29, CAL2, CaBP29K, 29 kDa calbindin.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAGPQQQPPY LHLAELTASQ FLEIWKHFDA DGNGYIEGKE LENFFQELEK ARKGSGMMSK SDNFGEKMKE FMQKYDKNSD GKIEMAELAQ ILPTEENFLL CFRQHVGSST EFMEAWRKYD TDRSGYIEAN ELKGFLSDLL KKANRPYDEP KLQEYTQTIL RMFDLNGDGK LGLSEMSRLL PVQENFLLKF QGMKLTSEEF NAIFTFYDKD RSGYIDEHEL DALLKDLYEK NKKEMNIQQL TNYRKSVMSL AEAGKLYRKD LEIVLCSEPP M.

    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.

    Calb2 Human
  • View Data Sheet

    Name :

    G6PD Human

    Description:

    Glucose-6-Phosphate Dehydrogenase Human Recombinant

    G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    Product # :

    ENZ-608

    Price :

    Quantity :

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    Description

    G6PD Human Recombinant produced in Hi-5 cells is a single polypeptide chain containing 535 amino acids (1-515) and having a molecular mass of 61.4kDa.G6PD is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Hi-5 cells.

    Formulation

    The G6PD solution (0.5mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.1mM PMSF, 2mM EDTA, 2mM DTT, 200mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Biological Activity

    Specific activity is > 45 units/ml obtained by measuring the increase of beta-NADPH in absorbance at 340 nm resulting from the reduction of beta NADP. One unit oxidizes 1.0 umole D-glucose-6-phosphate to 6-phospho-D-gluconate per min in the presence of beta-NADP at pH 7.4 at 25C.

    Citations

    More Info

    • Introduction

      G6PD is the rate-limiting enzyme of the pentose phosphate pathway, a metabolic pathway that supplies reducing energy to cells by maintaining the level of NADPH. G6PD converts glucose-6-phosphate into 6-phosphoglucono-?-lactone and at the same time produces NADPH. The NADPH maintains the level of glutathione in these cells that helps protect the red blood cells against oxidative damage. G6PD deficiency causes acute hemolytic anemia, neonatal jaundice or acute hemolysis. G6PD is a cytosolic enzyme encoded by an X-linked gene whose main function is to produce NADPH, a crucial electron donor in the defense against oxidizing agents and in reductive biosynthetic reactions. G6PD produces pentose sugars for nucleic acid synthesis and is a main producer of NADPH reducing power.

    • Synonyms

      G6PD, G6PD1, Glucose-6-phosphate 1-dehydrogenase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MAEQVALSRT QVCGILREEL FQGDAFHQSD THIFIIMGAS GDLAKKKIYP TIWWLFRDGL LPENTFIVGY ARSRLTVADI RKQSEPFFKA TPEEKLKLED FFARNSYVAG QYDDAASYQR LNSHMNALHL GSQANRLFYL ALPPTVYEAV TKNIHESCMS QIGWNRIIVE KPFGRDLQSS DRLSNHISSL FREDQIYRID HYLGKEMVQN LMVLRFANRI FGPIWNRDNI ACVILTFKEP FGTEGRGGYF DEFGIIRDVM QNHLLQMLCL VAMEKPASTN SDDVRDEKVK VLKCISEVQA NNVVLGQYVG NPDGEGEATK GYLDDPTVPR GSTTATFAAV VLYVENERWD GVPFILRCGK ALNERKAEVR LQFHDVAGDI FHQQCKRNEL VIRVQPNEAV YTKMMTKKPG MFFNPEESEL DLTYGNRYKN VKLPDAYERL ILDVFCGSQM HFVRSDELRE AWRIFTPLLH QIELEKPKPI PYIYGSRGPT EADELMKRVG FQYEGTYKWV NPHKL

    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.

    G6Pd Human
  • View Data Sheet

    Name :

    LOX Human

    Description:

    Lysyl Oxidase Human Recombinant

    Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.

    Product # :

    ENZ-829

    Price :

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    Description

    LOX Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 272 amino acids (169-417a.a) and having a molecular mass of 31.4kDa.LOX is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 85% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lysyl Oxidase also known as LOX is an extracellular copper enzyme which initiates the crosslinking of collagens and elastin. LOX catalyzes oxidative deamination of the epsilon-amino group in certain lysine and hydroxylysine residues of collagens and lysine residues of elastin. Adding up to crosslinking extracellular matrix proteins, LOX plays a part in tumor suppression. Moreover, defects in LOX are the cause of autosomal recessive cutis laxa type I, CL type I. Two transcript variants encoding dissimilar isoforms have been found for LOX.

    • Synonyms

      Lysyl Oxidase, EC 1.4.3.13, Protein-lysine 6-oxidase, Lysyl oxidase.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSDDPYNPY KYSDDNPYYN YYDTYERPRP GGRYRPGYGT GYFQYGLPDL VADPYYIQAS TYVQKMSMYN LRCAAEENCL ASTAYRADVR DYDHRVLLRF PQRVKNQGTS DFLPSRPRYS WEWHSCHQHY HSMDEFSHYD LLDANTQRRV AEGHKASFCL EDTSCDYGYH RRFACTAHTQ GLSPGCYDTY GADIDCQWID ITDVKPGNYI LKVSVNPSYL VPESDYTNNV VRCDIRYTGH HAYASGCTIS PY.

    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.

    Lox Human
  • View Data Sheet

    Name :

    UROD Human

    Description:

    Uroporphyrinogen Decarboxylase Human Recombinant

    UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.

    Product # :

    ENZ-536

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    Description

    UROD Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 387 amino acids (1-367 a.a.) and having a molecular mass of 43 kDa. The UROD is fused to 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    UROD Human solution containing 20mM Tris pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UROD is the fifth enzyme in the human heme biosynthetic pathway and is in charge for the transfer of uroporphyrinogen to coproporphyrinogen through the deletion of four carboxymethyl side chains. UROD Mutations and deficiency result in 3 autosomal disorders in humans: familial porphyria cutanea tarda (f-PCT), sporadic porphyria cutanea tarda (s-PCT) and hepatoerythropoietic porphyria (HEP).

    • Synonyms

      UPD, PCT, EC 4.1.1.37, URO-D, UROD, Uroporphyrinogen Decarboxylase.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MEANGLGPQG FPELKNDTFL RAAWGEETDY TPVWCMRQAG RYLPEFRETR AAQDFFSTCR SPEACCELTL QPLRRFPLDA AIIFSDILVV PQALGMEVTM VPGKGPSFPE PLREEQDLER LRDPEVVASE LGYVFQAITL TRQRLAGRVP LIGFAGAPWT LMTYMVEGGG SSTMAQAKRW LYQRPQASHQ LLRILTDALV PYLVGQVVAG AQALQLFESH AGHLGPQLFN KFALPYIRDV AKQVKARLRE AGLAPVPMII FAKDGHFALE ELAQAGYEVV GLDWTVAPKK ARECVGKTVT LQVNLDPCAL YASEEEIGQL VKQMLDDFGP HRYIANLGHG LYPDMDPEHV GAFVDAVHKH SRLLRQN.

    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.

    Urod Human
  • View Data Sheet

    Name :

    MAP1LC3B Human

    Description:

    Microtubule-Associated Protein 1 Light Chain 3 Beta Human Recombinant

    Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    Product # :

    PRO-076

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    Description

    MAP1LC3B produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-120a.a.) and having a molecular mass of 16.2kDa.MAP1LC3B is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The MAP1LC3B protein solution (0.5mg/1ml) is formulated in 20mM Tris-HCl buffer (pH8.0)
    1mM DTT, 100mM NaCl and 20% glycerol.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      MAP1LC3B is a member of the MAP1 LC3 family. MAP1LC3B is a subunit of neuronal microtubule-associated MAP1A and MAP1B proteins, that are involved in microtubule assembly and important for neurogenesis. In addition, MAP1LC3B takes part in formation of autophagosomal vacuoles and is expressed mainly in heart, testis, brain and skeletal muscle.

    • Synonyms

      Microtubule-Associated Protein 1 Light Chain 3 beta, ATG8F, Autophagy-related ubiquitin-like modifier LC3 B, MAP1 light chain 3-like protein 2, MAP1A/MAP1B LC3 B, LC3B, MAP1A/1BLC3, MAP1ALC3.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPSEKTFKQR RTFEQRVEDV RLIREQHPTK IPVIIERYKG EKQLPVLDKT KFLVPDHVNM SELIKIIRRR LQLNANQAFF LLVNGHSMVS VSTPISEVYE SEKDEDGFLY MVYASQETFG

    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.

    Map1Lc3B Human
  • View Data Sheet

    Name :

    COQ9 Human

    Description:

    Coenzyme Q9 Human Recombinant

    Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.

    Product # :

    ENZ-898

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    Description

    COQ9 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 297 amino acids (45-318 a.a) and having a molecular mass of 33.3kDa.COQ9 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    COQ9 protein solution (1mg/ml) in Phosphate buffered saline (pH7.4), 10% glycerol and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Ubiquinone biosynthesis protein COQ9 (COQ9) represents a mitochondrial ubiquinone biosynthesis gene. The COQ9 protein is likely required for biosynthesis of coenzyme Q10, since mutations at this locus have been linked with autosomal-recessive neonatal-onset primary coenzyme Q10 deficiency.

    • Synonyms

      Ubiquinone biosynthesis protein COQ9, mitochondrial, C16orf49, COQ10D5, C16orf49, HSPC326, PSEC0129.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSRSSDEQK QQPPNSFSQQ HSETQGAEKP DPESSHSPPR YTDQGGEEEE DYESEEQLQH RILTAALEFV PAHGWTAEAI AEGAQSLGLS SAAASMFGKD GSELILHFVT QCNTRLTRVL EEEQKLVQLG QAEKRKTDQF LRDAVETRLR MLIPYIEHWP RALSILMLPH NIPSSLSLLT SMVDDMWHYA GDQSTDFNWY TRRAMLAAIY NTTELVMMQD SSPDFEDTWR FLENRVNDAM NMGHTAKQVK STGEALVQGL MGAAVTLKNL TGLNQRR.

    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.

    Coq9 Human
  • View Data Sheet

    Name :

    Collagen-I Goat

    Description:

    Goat Collagen-I

    Product # :

    PRO-2682

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    Description

    Goat Collagen-I is a natural protein purified from Goat tissues. Collagen-I is purified by proprietary chromatographic techniques.

    Source

    Goat tissues.

    Formulation

    Collagen-I was lyophilized without additives.

    Purity

    Greater than 90.0% as determined by SDS-PAGE 90.0%.

    Citations

    More Info

    • Introduction

      Collagen, a major component of the extracellular matrix, is a fibrous protein that provides tensile strength to tissues giving them structural integrity. Collagen and its derivative, gelatin, have been widely used in medical, pharmaceutical and consumer products for more than 100 years. The supply of these materials, created from animal remains, is both abundant and inexpensive. However, most formulations are not highly purified and have the potential to cause an inflammatory reaction in some product users. In addition, concerns have been raised over the last several years about the potential for contamination of bovine products with the agent that causes mad cow disease and its human variant, Creutzfeldt-Jakob Disease. Animal collagens are subject to extensive modifications that continue over the life of the molecule in the extracellular space. These differences influence both the extractability of collagens from tissue and the biophysical characteristics of these collagens. As a result, collagens isolated from tissues exhibit significant lot-to-lot variability and, as bulk materials, are often analytically intractable. Products that contain animal-derived collagen can induce potentially harmful inflammatory or immune responses in humans and pose risk of contamination with viruses or prions, potentially life-threatening pathogens. Recombinant collagens are essentially identical to the native collagen protein thereby reducing the risk of inflammation, immune response, and disease as compared to animal-sourced collagen.

    • Physical Appearance

      Filtered White lyophilized (freeze-dried) powder.

    • Stability

      Lyophilized Collagen-I although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution Collagen-I should be stored at 4C between 2-7 days and for future use below -18C.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 Add 0.5 M acetic acid, pH 2.5 to prepare a working stock solution not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Collagen I Goat
  • View Data Sheet

    Name :

    lldD E. coli

    Description:

    L-Lactate Dehydrogenase E.Coli Recombinant

    L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.

    Product # :

    ENZ-618

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    Description

    lldD E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 45.3kDa.lldD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

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

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      L-lactate dehydrogenase (lldD) is present in a various organisms, including plants and animals. lldD is an oxidoreductase which catalyses the interconversion of pyruvate and lactate with concurrent interconversion of NADH and NAD+. Seeing that lldD can catalyze the oxidation of hydroxybutyrate, it is occasionally called Hydroxybutyrate Dehydrogenase (HBD).

    • Synonyms

      L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMIISAA SDYRAAAQRI LPPFLFHYMD GGAYSEYTLR RNVEDLSEVA LRQRILKNMS DLSLETTLFN EKLSMPVALA PVGLCGMYAR RGEVQAAKAA DAHGIPFTLS TVSVCPIEEV APAIKRPMWF QLYVLRDRGF MRNALERAKA AGCSTLVFTV DMPTPGARYR DAHSGMSGPN AAMRRYLQAV THPQWAWDVG LNGRPHDLGN ISAYLGKPTG LEDYIGWLGN NFDPSISWKD LEWIRDFWDG PMVIKGILDP EDARDAVRFG ADGIVVSNHG GRQLDGVLSS ARALPAIADA VKGDIAILAD SGIRNGLDVV RMIALGADTV LLGRAFLYAL ATAGQAGVAN LLNLIEKEMK VAMTLTGAKS ISEITQDSLV QGLGKELPAA LAPMAKGNAA.

    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.

    Lldd E Coli
  • View Data Sheet

    Name :

    HDGF2 Human

    Description:

    Hepatoma-Derived Growth Factor-2 Human Recombinant

    Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

    Product # :

    CYT-132

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    Description

    HDGF2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-203 a.a.) and having a molecular mass of 25.1kDa (Molecular weight on SDS-PAGE will appear higher). HDGF2 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HDGF2 protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 8.0), 1mM DTT, 10% glycerol and 0.1M NaCl.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    SDS-PAGE

    HDGF2 Human - Product image 1

    Citations

    More Info

    • Introduction

      Hepatoma-derived growth factor, related protein 3 (HDGFRP3/HDGF2) is the original member of a family of polypeptides labeled HDGF related proteins (HRPs). The HDGF2 protein augments DNA synthesis and may play a part in cell proliferation. HDGF2 is expressed primarily in the testis and the brain, to an intermediate extent in the heart, and to a slight extent in the ovaries, kidneys, spleen, and liver in humans.

    • Synonyms

      Hepatoma-derived growth factor-related protein 3, HRP-3, Hepatoma-derived growth factor 2, HDGF-2, HDGFRP3, HDGF2, CGI-142.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
      KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

    • Background

      What is the molecular weight/Mw of HDGF2 HUMAN Protein?
      HDGF2 HUMAN Protein has a total Mw of 25.1kDa.

      What is the source or expression system of HDGF2 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of HDGF2 HUMAN Protein?
      HDGF2 HUMAN Protein is >90% pure as determined by SDS-PAGE.

      What is the Biological Activity of HDGF2 HUMAN Protein?
      The biological functionality of HDGF2 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of HDGF2 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSHMARPRP REYKAGDLVF AKMKGYPHWP ARIDELPEGA VKPPANKYPI FFFGTHETAF LGPKDLFPYK EYKDKFGKSN KRKGFNEGLW EIENNPGVKF TGYQAIQQQS SSETEGEGGN TADASSEEEG DRVEEDGKGK RKNEKAGSKR KKSYTSKKSS
      KQSRKSPGDE DDKDCKEEEN KSSSEGGDAG NDTRNTTSDL QKTSEGT.

      What applications can HDGF2 HUMAN Protein be used in?
      HDGF2 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HDGF2 HUMAN Protein?
      The endotoxin level is minimal, HDGF2 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.

    Hdgf2 Human
  • View Data Sheet

    Name :

    TK1 Human

    Description:

    Thymidine Kinase 1 Human Recombinant

    Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    Product # :

    PKA-036

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    Description

    TK1 Human Recombinant produced in E. coli is a single polypeptide chain containing 258 amino acids (1-234) and having a molecular mass of 28.0 kDa.TK1 is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The TK1 solution (1mg/1ml) contains 20mM Tris-HCl buffer (pH 8.0), 100mM NaCl, 1mM DTT and 20% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Thymidine Kinase 1 (TK1) is a phosphotransferase (a kinase): 2'-deoxythymidine kinase, ATP-thymidine 5'-phosphotransferase. TK1 is present in 2 forms in mammalian cells, TK1 and TK2. Thymidine kinases hold a main function in the synthesis of DNA and thus in cell division, as they are part of the distinctive reaction chain to introduce deoxythymidine (present in the body fluids as a result of degradation of DNA from food and from dead cells) into the DNA. Thymidine kinase is necessary for the action of many antiviral drugs. Thymidine kinase is used to select hybridoma cell lines in production of monoclonal antibodies.

    • Synonyms

      Thymidine kinase 1 soluble, thymidine kinase cytosolic, TK2, EC 2.7.1.21.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMSCINL PTVLPGSPSK TRGQIQVILG PMFSGKSTEL MRRVRRFQIA QYKCLVIKYA KDTRYSSSFC THDRNTMEAL PACLLRDVAQ EALGVAVIGI DEGQFFPDIV EFCEAMANAG KTVIVAALDG TFQRKPFGAI LNLVPLAESV VKLTAVCMEC FREAAYTKRL GTEKEVEVIG GADKYHSVCR LCYFKKASGQ PAGPDNKENC PVPGKPGEAV AARKLFAPQQ ILQCSPAN.

    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.

    Tk1 Human
  • View Data Sheet

    Name :

    Lysozyme Human

    Description:

    Lysozyme Human Recombinant

    EC 3.2.1.17, LYZ, Lysozyme.

    Product # :

    ENZ-1159

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    Description

    Recombinant Human Lysozyme produced in Plant is a non-glycosylated, polypeptide chain containing 130 amino acids and having a molecular mass of 14.7kDa. The Recombinant Human Lysozyme is purified by proprietary chromatographic techniques.

    Source

    Oryza sativa (rice).

    Formulation

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

    Purity

    Purity as determined by SDS-PAGE is greater than 90%.

    Biological Activity

    1.6x105 U/mg.

    Citations

    More Info

    • Introduction

      Lysozymeis an antimicrobial enzyme produced by animals that are part of the innate immune system. Lysozyme is a glycoside hydrolase that catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan, which is the major component of gram-positive bacterial cell wall.Lysozymes have primarily a bacteriolytic function - those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.

    • Synonyms

      EC 3.2.1.17, LYZ, Lysozyme.

    • Physical Appearance

      Sterile Filtered lyophilized (freeze-dried) off white powder.

    • Stability

      Store the lyophilized Lysozyme between 2-8°C, do not freeze. Upon reconstitution Lysozyme should be stored at 4°C between 2-7 days and for future use below -18°C. Please prevent freeze-thaw cycles.

    • Solubility

      Stock solutions can be prepared by dissolving gently into PBS for several minutes. Recommended stock concentrations are 1mg/ml in PBS.

    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.

    Lysozyme Human
  • View Data Sheet

    Name :

    Deslorelin

    Description:

    Deslorelin

    Product # :

    HOR-240

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    Description

    Deslorelin is a potent LHRH/GnRH agonist has a molecular formula of C64H83N17O12, pGlu-His-Trp-Ser-Tyr-D-Trp-Leu-Arg-Pro-NHC2H5 having an Mw of 1284.4 Dalton.

    Formulation

    The Deslorelin peptide was lyophilized with no additives.

    Purity

    Greater than 99.0% as determined by RP-HPLC.

    Citations

    More Info

    • Introduction

      Deslorelin is being studied in the treatment of cancer as a way to block sex hormones made by the ovaries or testicles. It belongs to the family of drugs called gonadotropin-releasing hormone analogs. It is used for the induction of ovulation in mares. Deslorelin binds to and activates pituitary gonadotropin releasing hormone (GnRH) receptors. Continuous, prolonged administration of goserelin in males results in pituitary GnRH receptor desensitization and inhibition of pituitary secretion of follicle stimulating hormone (FSH) and luteinizing hormone (LH), leading to a significant decline in testosterone production; in females, prolonged administration results in a decrease in estradiol production.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

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

    Deslorelin
  • View Data Sheet

    Name :

    F9 Human

    Description:

    Coagulation Factor IX Human

    Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.

    Product # :

    PRO-353

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    Description

    Human Factor-IX produced from fresh frozen human plasma is a glycosylated polypeptide chain having a molecular mass of 56 kDa.

    Source

    Human Plasma.

    Formulation

    The Factor-IX is provided in a sterile solution containing 20mM Tris-HCl pH-7.4, 100mM NaCl and 1mM Benzamidine.

     

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Biological Activity

    The activity per mg was tested and found to be 380 PEU/mg.

    Citations

    More Info

    • Introduction

      Human Factor IX also called Christmas-Factor is a glycoprotein, which is synthesized in the liver and belongs to the serine proteases system and is part of the S1 peptidase family.
      Lack of Factor-IX causes Hemophilia-B meaning Christmas Disease. Factor-IX has a N-terminus region which contains 12xGla residues which asist the calcium dpendant binding of Factor-IX to the phospholipid surface. Factor-IX is activated by either factor XIa or the factor VIIa/tissue factor/phospholipid complex. Cleavage yields the intermediate IXa, which is subsequently converted to the fully active form IXab.
      Factor-IX binds initially to exosites on the factor XIa heavy chain, followed by interaction at the active site with subsequent bond cleavage. Coagulation factor IX is activated by interaction with the erythrocyte membrane, causing intrinsic coagulation. Chaperones & lectins act simultaniously to guarantee the proper folding of Factor-IX and the retention of mutant molecules. Human Factor IX, activated by either the Contact or Tissue Factor Pathway, is responsible for the activation of Factor X to Xa.

    • Synonyms

      Coagulation factor IX, EC 3.4.21.22, Christmas factor, Plasma thromboplastin component, PTC, F9, FIX, HEMB, MGC129641, MGC129642, GLA domain, Factor IX.

    • 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. Please prevent freeze-thaw cycles..

    • Human Virus Test

      Human plasma was tested and found negative for HIV-1, HIV-2, Hepatitis B Surface antigen and HCV. Donors are screened for CJD (Creutzfeldt-Jakob Disease).

    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.

    Factor Ix Human
  • View Data Sheet

    Name :

    HDGFL1 Human

    Description:

    Hepatoma Derived Growth Factor-Like 1 Human Recombinant

    Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.

    Product # :

    CYT-850

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    Description

    HDGFL1 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 274 amino acids (1-251 a.a) and having a molecular mass of 29.6kDa.HDGFL1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    HDGFL1 protein solution (0.25mg/ml) containing Phosphate buffered saline, (pH7.4) and 10% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Hepatoma Derived Growth Factor-Like 1 (HDGFL1) is a member of the HDGF family and contains 1 PWWP domain.

    • Synonyms

      Hepatoma-derived growth factor-like protein 1, DJ309H15.1, PWWP1, PWWP domain-containing protein 1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

    • Background

      What is the molecular weight/Mw of HDGFL1 HUMAN Protein?
      HDGFL1 HUMAN Protein has a total Mw of 29.6kDa.

      What is the source or expression system of HDGFL1 HUMAN Protein?
      Escherichia Coli.

      What is the Purity of HDGFL1 HUMAN Protein?
      HDGFL1 HUMAN Protein is >95% pure as determined by SDS-PAGE.

      What is the Biological Activity of HDGFL1 HUMAN Protein?
      The biological functionality of HDGFL1 HUMAN Protein will be determined in the future.

      What is the amino acid sequence of HDGFL1 HUMAN Protein?
      MGSSHHHHHH SSGLVPRGSH MGSMSAYGMP MYKSGDLVFA KLKGYAHWPA RIEHMTQPNR YQVFFFGTHE TAFLSPKRLF PYKECKEKFG KPNKRRGFSA GLWEIENNPT VQASDCPLAS EKGSGDGPWP EPEAAEGDED KPTHAGGGGD ELGKPDDDKP TEEEKGPLKR SAGDPPEDAP KRPKEAAPDQ EEEAEAERAA EAERAAAAAA ATAVDEESPF LVAVENGSAP SEPGLVCEPP QPEEEELREE EVADEEASQE WHAEAPGGGD RDSL.

      What applications can HDGFL1 HUMAN Protein be used in?
      HDGFL1 HUMAN Protein can probably be used in western blot, ELISA and Lateral Flow.

      What is the endotoxin level for HDGFL1 HUMAN Protein?
      The endotoxin level is minimal, HDGFL1 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.

    Hdgfl1 Human
  • View Data Sheet

    Name :

    LTF Holo Human

    Description:

    Lactoferrin Holo Human Recombinant

    Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    Product # :

    PRO-592

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    Description

    Recombinant Human Holo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Holo Lactoferrin is purified by proprietary chromatographic techniques.

    Source

    Rice Flour.

    Formulation

    The Human Holo lactoferrin was lyophilized with no additives.

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Lactoferrin is a glycoprotein that belongs to the transferrin family of iron binding proteins. It is found in human breast milk as well as most epithelial surface secretions including tears, nasogastric, saliva, and bronchial. Lactoferrin binds 2 molecules of iron with very high affinity. Lactoferrin inhibits bacterial growth by withholding iron, its N-terminal region is an antimicrobial peptide. Lactotransferrin acts synergistically with lysozyme to potentiate the activity of both proteins. The multifunctional protein lactoferrin has many physiological possible roles. It is often referred to as an innate defense protein and frequently serves as the first line of defense in protection against pathogens. It has been shown to have the ability to bind iron, it is a natural anti-bacterial, anti-fungal and anti-viral, it is an antioxidant and it also has immunomodulatory properties. It has many beneficial properties, which make it a good candidate for a number of product applications. Considerable research is currently going on to explain the various suggested biological functions of lactoferrin.

    • Synonyms

      Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.

    • Physical Appearance

      Pink lyophilized powder.

    • Stability

      Recombinant Holo Lactoferrin although stable at room temperature for 5 days, should be stored desiccated below -18°C.Please prevent freeze-thaw cycles.

    • Solubility

      It is recommended to reconstitute the lyophilized LTF Holo Human in sterile water at 10mg/ml, which can then be further diluted to other aqueous solutions.

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

    Lactoferrin Holo Human
  • View Data Sheet

    Name :

    PYGL Human

    Description:

    Phosphorylase, Glycogen, Liver Human Recombinant

    GSD6, Glycogen phosphorylase, liver form.

    Product # :

    ENZ-675

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    Description

    PYGL Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 879 amino acids (1-847 a.a) and having a molecular mass of 100.7kDa.PYGL is fused to a 32 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    PYGL protein solution (0.25mg/ml) in phosphate buffered saline (pH7.4), 30% glycerol and 1mM DTT.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Glycogen phosphorylase (PYGL) converts from inactive phosphorylase B to active phosphorylase A by phosphorylation of serine residue 15. Activity of the PYGL enzyme is further regulated by numerous allosteric effectors and hormonal controls. The liver isozyme supplies the glycemic demands of the body in general whereas the brain and muscle isozymes supply just those tissues.

    • Synonyms

      GSD6, Glycogen phosphorylase, liver form.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSEFELRRQ ASMAKPLTDQ EKRRQISIRG IVGVENVAEL KKSFNRHLHF TLVKDRNVAT TRDYYFALAH TVRDHLVGRW IRTQQHYYDK CPKRVYYLSL EFYMGRTLQN TMINLGLQNA CDEAIYQLGL DIEELEEIEE DAGLGNGGLG RLAACFLDSM ATLGLAAYGY GIRYEYGIFN QKIRDGWQVE EADDWLRYGN PWEKSRPEFM LPVHFYGKVE HTNTGTKWID TQVVLALPYD TPVPGYMNNT VNTMRLWSAR APNDFNLRDF NVGDYIQAVL DRNLAENISR VLYPNDNFFE GKELRLKQEY FVVAATLQDI IRRFKASKFG STRGAGTVFD AFPDQVAIQL NDTHPALAIP ELMRIFVDIE KLPWSKAWEL TQKTFAYTNH TVLPEALERW PVDLVEKLLP RHLEIIYEIN QKHLDRIVAL FPKDVDRLRR MSLIEEEGSK RINMAHLCIV GSHAVNGVAK IHSDIVKTKV FKDFSELEPD KFQNKTNGIT PRRWLLLCNP GLAELIAEKI GEDYVKDLSQ LTKLHSFLGD DVFLRELAKV KQENKLKFSQ FLETEYKVKI NPSSMFDVQV KRIHEYKRQL LNCLHVITMY NRIKKDPKKL FVPRTVIIGG KAAPGYHMAK MIIKLITSVA DVVNNDPMVG SKLKVIFLEN YRVSLAEKVI PATDLSEQIS TAGTEASGTG NMKFMLNGAL TIGTMDGANV EMAEEAGEEN LFIFGMRIDD VAALDKKGYE AKEYYEALPE LKLVIDQIDN GFFSPKQPDL FKDIINMLFY HDRFKVFADY EAYVKCQDKV SQLYMNPKAW NTMVLKNIAA SGKFSSDRTI KEYAQNIWNV EPSDLKISLS NESNKVNGN.

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    Pygl Human
  • View Data Sheet

    Name :

    Leptin Rat, PEG

    Description:

    Pegylated Rat Leptin Recombinant

    OB Protein, Obesity Protein, OBS, Obesity factor.

    Product # :

    CYT-592

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    Description

    Mono-Pegylated Leptin Rat Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 146 amino acids and an additional Ala at N-terminus having a molecular mass of 35.6 kDa (with 20 kDa PEG) as determined by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as 48 kDa protein and in gel-filtration on Superdex 200 as over 100 kDa protein. Its half-life in circulation after SC injection was over 20 hours. Rat Leptin was purified by proprietary chromatographic techniques according to Salomon et al (2006) Protein Expression and Purification 47, 128–136 and then pegylated.

    Source

    Escherichia Coli.

    Formulation

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

    Purity

    Greater than 99.0% as determined by:
    (a) Analysis by Gel-Filtration.
    (b) Analysis by SDS-PAGE.

    Biological Activity

    Pegylated Rat Leptin is capable of stimulatng proliferation of BAF/3 cells stably transfected with the long form of human leptin receptor. Its in vitro activity is only slightly lower than the non-pegylated antagonist but in vivo it has profound weight reducing effect (as compared to the non-pegylated leptin), resulting mainly from reduced food intake.

    Citations

    More Info

    • Introduction

      A 16-kDa peptide hormone secreted from white adipocytes and implicated in the regulation of food intake and energy balance. Leptin provides the key afferent signal from fat cells in the feedback system that controls body fat stores.

    • Synonyms

      OB Protein, Obesity Protein, OBS, Obesity factor.

    • Physical Appearance

      Sterile Filtered White lyophilized (freeze-dried) powder.

    • Stability

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

    • Solubility

      It is recommended to reconstitute the lyophilized pegylated Rat Leptin in sterile water or in sterile 0.4% NaHCO3 adjusted to pH-8.5, not less than 100µg/ml, which can then be further diluted to other aqueous solutions.

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

    Leptin Rat Pegylated
  • View Data Sheet

    Name :

    SDSL Human

    Description:

    Serine Dehydratase-Like Human Recombinant

    Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

    Product # :

    ENZ-180

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    Description

    SDSL Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-329) and having a molecular mass of 37.3 kDa.SDSL is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    E.coli.

    Formulation

    The SDSL solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 2mM DTT, 0.1M NaCl and 10% glycerol.

    Purity

    Greater than 90% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SDSL belongs to the serine/threonine dehydratase family and function as a serinespecific dehydratase. SDSL utilizes pyridoxal phosphate and is one of three key enzymes which take part in the metabolism of Glycine and serine.

    • Synonyms

      Serine dehydratase-like, SDS-RS1, Serine dehydratase 2, TDH, L-serine dehydratase/L-threonine deaminase, SDH 2, serine dehydratase related sequence 1, EC 4.3.1.17, EC 4.3.1.19.

    • Physical Appearance

      Sterile Filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MGSHMDGPVA EHAKQEPFHV VTPLLESWAL SQVAGMPVFL KCENVQPSGS FKIRGIGHFC QEMAKKGCRH LVCSSGGNAG IAAAYAARKL GIPATIVLPE STSLQVVQRL QGEGAEVQLT GKVWDEANLR AQELAKRDGW ENVPPFDHPL IWKGHASLVQ ELKAVLRTPP GALVLAVGGG GLLAGVVAGL LEVGWQHVPI IAMETHGAHC FNAAITAGKL VTLPDITSVA KSLGAKTVAA RALECMQVCK IHSEVVEDTE AVSAVQQLLD DERMLVEPAC GAALAAIYSG LLRRLQAEGC LPPSLTSVVV IVCGGNNINS RELQALKTHL GQV.

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    Sdsl Human
  • View Data Sheet

    Name :

    SLPI Human

    Description:

    Secretory Leukocyte Peptidase Inhibitor Human Recombinant

    Antileukoproteinase, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, WAP four-disulfide core domain protein 4, Protease inhibitor WAP4, Seminal proteinase inhibitor, Mucus proteinase inhibitor.

    Product # :

    PRO-849

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    Description

    SLPI Recombinant E.coli produced in E.Coli is a single, non-glycosylated polypeptide chain containing 128 amino acids (26-132 a.a.) and having a molecular mass of 14 kDa. The SLPI is fused to a 21 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    SLPI Human solution containing 20mM Tris-HCl pH-8.0, 2mM DTT, 0.1M NaCl & 20% glycerol.

    Purity

    Greater than 80.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      SLPI is a secreted inhibitor which guards epithelial tissues from serine proteases. SLPI is localized in various secretions including seminal plasma, cervical mucus, and bronchial secretions, and has affinity for trypsin, leukocyte elastase, and cathepsin G. SLPI inhibitory effect contributes to the immune response by protecting epithelial surfaces from attack by endogenous proteolytic enzymes. SLPI protein has broad-spectrum anti-biotic activity. SLPI is an acid-stable proteinase inhibitor with strong affinities for trypsin, chymotrypsin, elastase, and cathepsin G. SLPI prevents elastase-mediated damage to oral and mucosal tissues.

    • Synonyms

      Antileukoproteinase, ALK1, ALP, BLPI, HUSI, HUSI-I, MPI, WAP4, WFDC4, WAP four-disulfide core domain protein 4, Protease inhibitor WAP4, Seminal proteinase inhibitor, Mucus proteinase inhibitor.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MSGKSFKAGV CPPKKSAQCL RYKKPECQSD WQCPGKKRCC PDTCGIKCLD PVDTPNPTRR KPGKCPVTYG QCLMLNPPNF CEMDGQCKRD LKCCMGMCGK SCVSPVKA.

    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.

    Slpi Human
  • View Data Sheet

    Name :

    PODXL Mouse

    Description:

    Podocalyxin-Like Mouse Recombinant

    Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    Product # :

    PRO-2310

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    Description

    PODXL Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 391 amino acids (22-404a.a.) and having a molecular mass of 41.0kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). PODXL is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

    Source

    Sf9, Baculovirus cells.

    Formulation

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

    Purity

    Greater than 95% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      Podocalyxin (PODXL) is a greatly glycosylated transmembrane sialoprotein in the CD34 and endoglycan family. The PODXL protein is involved in the regulation of both adhesion and cell morphology and cancer progression. PODXL functions as an anti-adhesive molecule, which retains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Moreover, PODXL serves as a pro-adhesive molecule, enhancing the adherence of cells to immobilized ligands, increasing the rate of migration and cell-cell contacts in an integrin-dependent manner.

    • Synonyms

      Podocalyxin, Podocalyxin-like protein 1, PC, PCLP-1.

    • Physical Appearance

      Sterile Filtered clear solution.

    • Stability

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

    • Amino Acid Sequence

      HNGNETSTSA IKSSTVQSHQ SATTSTEVTT GHPVASTLAS TQPSNPTPFT TSTQSPSMPT STPNPTSNQS GGNLTSSVSE VDKTKTSSPS STAFTSSSGQ TASSGGKSGD SFTTAPTTTL GLINVSSQPT DLNTTSKLLS TPTTDNTTSP QQPVDSSPST ASHPVGQHTP AAVPSSSGST PSTDNSTLTW KPTTHKPLGT SEATQPLTSQ TPGITTLPVS TLQQSMASTV GTTTEEFTHL ISNGTPVAPP GPSTPSPIWA FGNYQLNCEP PIRPDEELLI LNLTRASLCE RSPLDEKEKL VELLCHSVKA SFKPAEDLCT LHVAPILDNQ AVAVKRIIIE TKLSPKAVYE LLKDRWDDLT EAGVSDMKLG KEGPPEVNED RFSLEHHHHH 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.

    Podxl Mouse
  • View Data Sheet

    Name :

    GIPC1 Human

    Description:

    GIPC PDZ Domain Member 1 Human Recombinant

    PDZ domain-containing protein GIPC1, GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, Tax interaction protein 2, TIP-2, GIPC1, C19orf3, GIPC, RGS19IP1, NIP, GIPC, IIP-1, SEMCAP, Hs.6454, MGC3774, GLUT1CBP, MGC15889. SYNECTIN, SYNECTIIN.

    Product # :

    PRO-855

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    Description

    GIPC1 Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 353 amino acids (1-333 a.a) and having a molecular mass of 38.2kDa. The GIPC1 is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    GIPC1 Human solution (0.5mg/ml) containing 20mM Tris-HCl pH-8, 1mM DTT, 0.1M NaCl, 1mM EDTA & 20% glycerol.

    Purity

    Greater than 95.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      GIPC1 is a PDZ domain protein that cooperates with RGS-GAIP and the viral oncoprotein TAX, which transactivates viral and cellular promoters throughout interactions with different transcription factors. GIPC1 particularly localizes to clusters of vesicles close to the plasma membrane and takes part in G protein-coupled signaling pathway participating in regulating Clathrin-coated vesicular trafficking. GIPC1 cooperates with membrane bound Semaphorin F, which is takes part in neuronal axon growth, and controls the subcellular distribution of M-SemF in the brain.

    • Synonyms

      PDZ domain-containing protein GIPC1, GAIP C-terminus-interacting protein, RGS-GAIP-interacting protein, RGS19-interacting protein 1, Tax interaction protein 2, TIP-2, GIPC1, C19orf3, GIPC, RGS19IP1, NIP, GIPC, IIP-1, SEMCAP, Hs.6454, MGC3774, GLUT1CBP, MGC15889. SYNECTIN, SYNECTIIN.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MPLGLGRRKK APPLVENEEA EPGRGGLGVG EPGPLGGGGS GGPQMGLPPP PPALRPRLVF HTQLAHGSPT GRIEGFTNVK ELYGKIAEAF RLPTAEVMFC TLNTHKVDMD KLLGGQIGLE DFIFAHVKGQ RKEVEVFKSE DALGLTITDN GAGYAFIKRI KEGSVIDHIH LISVGDMIEA INGQSLLGCR HYEVARLLKE LPRGRTFTLK LTEPRKAFDM ISQRSAGGRP GSGPQLGTGR GTLRLRSRGP ATVEDLPSAF EEKAIEKVDD LLESYMGIRD TELAATMVEL GKDKRNPDEL AEALDERLGD FAFPDEFVFD VWGAIGDAKV GRY.

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    Gipc1 Human
  • View Data Sheet

    Name :

    UBE2D3 Human

    Description:

    Ubiquitin Conjugating Enzyme E2D3 Human Recombinant

    Ubiquitin-conjugating enzyme E2 D3, EC 6.3.2.19, Ubiquitin-protein ligase D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2-17 kDa 3, E2(17)KB 3, UBC4/5, UBCH5C, MGC5416, MGC43926, UBE2D3.

    Product # :

    ENZ-343

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    Description

    UBE2D3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 169 amino acids (1-149a.a.) and having a molecular mass of 19.1kDa. UBE2D3 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

    Source

    Escherichia Coli.

    Formulation

    The UBE2D3 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 40% glycerol, 0.15M NaCl and 1mM DTT.

    Purity

    Greater than 90.0% as determined by SDS-PAGE.

    Citations

    More Info

    • Introduction

      UBE2D3 enzymes are human homologs of the yeast UBC4/5 family and play many important regulatory roles in inflammation and cancer. UbcH5a mediates the degradation of a myriad of short-lived regulatory proteins (such as p53 in the presence of E6/E6-AP or MDM2, c-Fos, I?B?, p105) and abnormal proteins. UBE2D3 has 88% and 89% sequence identity with UbcH5a and UbcH5b respectively.

    • Synonyms

      Ubiquitin-conjugating enzyme E2 D3, EC 6.3.2.19, Ubiquitin-protein ligase D3, Ubiquitin carrier protein D3, Ubiquitin-conjugating enzyme E2-17 kDa 3, E2(17)KB 3, UBC4/5, UBCH5C, MGC5416, MGC43926, UBE2D3.

    • Physical Appearance

      Sterile filtered colorless solution.

    • Stability

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

    • Amino Acid Sequence

      MGSSHHHHHH SSGLVPRGSH MLSNRKCLSK ELSDLARDPP AQCSAGPVGD DMFHWQATIM GPNDSPYQGG VFFLTIHFPT DYPFKPPKVA FTTRIYHPNI NSNGSICLDI LRSQWSPALT ISKVLLSICS LLCDPNPDDP LVPEIARIYK TDRDKYNRIS REWTQKYAM.

    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.

    Ube2D3 Human
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