Search results
1000 results found for “Septin”
Name
Description
Product #
Price
Quantity
Shipping Method
- View Data Sheet
Name :
LXN MouseDescription:
Latexin Mouse Recombinant
Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.
Product # :
PRO-2218Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LXN Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 245 amino acids (1-222 a.a) and having a molecular mass of 27.9kDa. LXN is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
LXN protein solution (1mg/ml) containing Phosphate Buffer Saline (pH7.4), 30% glycerol and 1mM DTT.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lxn also known as Latexin is a member of the protease inhibitor I47 (latexin) family. Lxn's function is hardly reversible, non-competitive, as well as potent inhibitor of CPA1, CPA2 and CPA4. Furthermore, Lxn plays a role in inflammation. Among the diseases associated with LXN are endocervicitis and listeriosis.
-
Synonyms
Latexin, Endogenous carboxypeptidase inhibitor, ECI, Tissue carboxypeptidase inhibitor, TCI.
-
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 MGSMEIPPTH YAASRAASVA ENCINYQQGT PHKLFLVQTV QQASKEDIPG RGHKYHLKFS VEEIIQKQVT VNCTAEVLYP QMGQGSAPEV NFTFEGEIGK NPDEEDNTFY QSLMSLKRPL EAQDIPDNFG NVSPQMKPVQ HLAWVACGYV MWQNSTEDTW YKMLKIQTVK QVQRNDDFIE LDYTILLHDI ASQEIIPWQM QVLWHPQYGT KVKHNSRLPK EGQAE.
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 :
CNBP HumanDescription:
Cellular Nucleic Acid Binding Protein Human Recombinant
CNBP1, DM2, PROMM, RNF163, ZCCHC22, ZNF9, Cellular nucleic acid-binding protein, CNBP, Zinc finger protein 9.
Product # :
PRO-1371Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNBP Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 193 amino acids (1-170 a.a) and having a molecular mass of 21kDa. CNBP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
CNBP protein solution (0.5mg/ml) containing 20mM Tris-HCl buffer (pH 7.5), 0.2M NaCl, 20% glycerol and 1mM DTT.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Cellular nucleic acid-binding protein (CNBP) is a nucleic-acid binding protein with seven zinc-finger domains, which has a preference for binding single stranded DNA and RNA. CNBP serves in cap-independent translation of ornithine decarboxylase mRNA, and also in sterol-mediated transcriptional regulation. The expansion of A CCTG in CNBP protein’s first intron results in myotonic dystrophy type 2.
-
Synonyms
CNBP1, DM2, PROMM, RNF163, ZCCHC22, ZNF9, Cellular nucleic acid-binding protein, CNBP, Zinc finger protein 9.
-
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 MGSMSSNECF KCGRSGHWAR ECPTGGGRGR GMRSRGRGFQ FVSSSLPDIC YRCGESGHLA KDCDLQEDAC YNCGRGGHIA KDCKEPKRER EQCCYNCGKP GHLARDCDHA DEQKCYSCGE FGHIQKDCTK VKCYRCGETG HVAINCSKTS EVNCYRCGES GHLARECTIE ATA.
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 :
CNOT7 MouseDescription:
CCR4-NOT Transcription Complex, Subunit 7 Mouse Recombinant
CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.
Product # :
PRO-908Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CNOT7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 271 amino acids (1-248 a.a) and having a molecular mass of 31.1kDa.CNOT7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
CNOT7 protein solution (1mg/ml) containing 20mM Tris-HCl buffer (pH8.0), 20% glycerol and 1mM DTT.
Purity
Greater than 80.0% as determined by SDS-PAGE.
More Info
-
Introduction
CCR4-Not transcription complex, subunit 7 (CNOT7) is a ubiquitous transcription factor. CNOT7 is a component of the CCR4 complex which functions as a general transcription regulation complex. Furthermore, CNOT7 binds to an anti-proliferative protein, BTG1 (B-cell translocation protein 1), which negatively regulates cell proliferation.
-
Synonyms
CCR4-NOT transcription complex subunit 7, Cnot7, Caf1, Pop2, AU022737.
-
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 MGSMPAATVD HSQRICEVWA CNLDEEMKKI RQVIRKYNYV AMDTEFPGVV ARPIGEFRSN ADYQYQLLRC NVDLLKIIQL GLTFMNEQGE YPPGTSTWQF NFKFNLTEDM YAQDSIELLT TSGIQFKKHE EEGIETQYFA ELLMTSGVVL CEGVKWLSFH SGYDFGYLIK ILTNSNLPEE ELDFFEILRL FFPVIYDVKY LMKSCKNLKM FFEDHIDDAK YCGHLYGLGS GSSYVQNGTG NAYEEEASKQ S.
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 :
RAB7A HumanDescription:
RAB7A, Member RAS Oncogene Family Human Recombinant
RAB7A member RAS oncogene family, RAB7, ras-related protein Rab-7a, FLJ20819, PSN, CMT2B, PRO2706.
Product # :
PRO-077Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
RAB7A produced in E.Coli is a single, non-glycosylated polypeptide chain containing 227 amino acids (1-207a.a.) and having a molecular mass of 25.6kDa.RAB7A is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The RAB7A protein solution (0.5mg/ml) is formulated in 20mM Tris-HCl buffer (pH8.0), 1mM DTT, 100mM NaCl and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
RAB7A belongs to the Ras superfamily of small Rab GTPases. RAB7A connects with the RIPL effector protein to regulator membrane trafficking from early to late endosome and to lysosomes. RAB7A can also regulate growth receptor endocytic trafficking, degradation, maturation of phagosome and autophagic vacuoles.
-
Synonyms
RAB7A member RAS oncogene family, RAB7, ras-related protein Rab-7a, FLJ20819, PSN, CMT2B, PRO2706.
-
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 MTSRKKVLLK VIILGDSGVG KTSLMNQYVN KKFSNQYKAT IGADFLTKEV MVDDRLVTMQ IWDTAGQERF QSLGVAFYRG ADCCVLVFDV TAPNTFKTLD SWRDEFLIQA SPRDPENFPF VVLGNKIDLE NRQVATKRAQ AWCYSKNNIP YFETSAKEAI
NVEQAFQTIA RNALKQETEV ELYNEFPEPI KLDKNDRAKA SAESCSC.
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 :
CCL7 MouseDescription:
Monocyte Chemotactic Protein-3 Mouse Recombinant (CCL7)
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
Product # :
CHM-318Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Monocyte Chemotactic Protein-3 Mouse Recombinant produced in E.Coli is a non-glycosylated, Polypeptide chain containing 74 amino acids and having a molecular mass of 8510 Dalton. The MCP-3 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The protein was lyophilized from a concentrated (1mg/ml) sterile solution containing no additives.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
The specific activity as determined by the ability of Mouse MCP-3 to chemoattract Balb/C mouse spleen MNCs at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.More Info
-
Introduction
Chemokine (C-C motif) ligand 7 (CCL7) is a small cytokine known as a chemokine that was previously called monocyte-specific chemokine 3 (MCP3). Due to CCL7 possessing two adjacent N-terminal cysteine residues in its mature protein, it is classified among the subfamily of chemokines known as CC chemokines. CCL7 specifically attracts monocytes, and regulates macrophage function. It is produced by certain tumor cell lines and by macrophages. This chemokine is located on chromosome 17 in humans, in a large cluster containing many other CC chemokines and is most closely related to CCL2(previously called MCP1).
-
Synonyms
Small inducible cytokine A7, CCL7, Monocyte chemotactic protein 3, MCP-3, Monocyte chemoattractant protein 3, NC28, chemokine (C-C motif) ligand 7, FIC, MARC, MCP3, SCYA6, SCYA7, MGC138463, MGC138465.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized MCP-3 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution CCL7 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 Monocyte Chemotactic Protein-3 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
QPDGPNASTC CYVKKQKIPK RNLKSYRRIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTP TPKP.
-
Background
What is the molecular weight/Mw of CCL7 MOUSE Protein?
CCL7 MOUSE Protein has a total Mw of 8.51kDa.
What is the source or expression system of CCL7 MOUSE Protein?
Escherichia Coli.
What is the Purity of CCL7 MOUSE Protein?
CCL7 MOUSE Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of CCL7 MOUSE Protein?
The specific activity as determined by the ability of Mouse MCP-3 to chemoattract Balb/C mouse spleen MNCs at 10-100ng/ml corresponding to a Specific Activity of 10,000-100,000IU/mg.
What is the amino acid sequence of CCL7 MOUSE Protein?
QPDGPNASTC CYVKKQKIPK RNLKSYRRIT SSRCPWEAVI FKTKKGMEVC AEAHQKWVEE AIAYLDMKTP TPKP.
What applications can CCL7 MOUSE Protein be used in?
CCL7 MOUSE Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for CCL7 MOUSE Protein?
The endotoxin level is minimal, CCL7 MOUSE Protein was purified using conventional chromatography techniques.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
BD 2 HumanDescription:
Beta Defensin-2 Human Recombinant
BD-2, hBD-2, Defensin beta 2, Skin-antimicrobial peptide 1, SAP1, DEFB4, DEFB102, DEFB2, DEFB4P, Beta-defensin 2.
Product # :
CYT-571Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Beta Defensin-2 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 41 amino acids and having a molecular mass of 4.3 kDa. The BD-2 is purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The Human BD-2 was lyophilized from a 0.2µm filtered concentrated (1mg/ml) solution containing 20mM PB pH-7.4 and 130mM NaCl.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.Biological Activity
Determined by the ability to chemoattract human dendritic immature cells at a concentration of 10-100ng/ml.More Info
-
Synonyms
BD-2, hBD-2, Defensin beta 2, Skin-antimicrobial peptide 1, SAP1, DEFB4, DEFB102, DEFB2, DEFB4P, Beta-defensin 2.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Beta Defensin-2 Recombinant although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution BD-2 should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized Beta Defensin-2 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P.
-
Background
Beta Defensin-2 Human Recombinant: Unveiling its Role in Innate Immunity and Therapeutic Potential
Abstract:
Beta Defensin-2 (BD-2), a member of the defensin family, plays a crucial role in innate immunity and host defense. This research paper provides an overview of BD-2 human recombinant, exploring its molecular characteristics, antimicrobial properties, and therapeutic applications. Understanding the multifaceted role of BD-2 offers new avenues for developing innovative immunotherapies. This article offers a concise analysis of BD-2, highlighting its impact on innate immunity and its therapeutic potential.Introduction:
Innate immunity serves as the first line of defense against invading pathogens. BD-2, a key antimicrobial peptide within the defensin family, plays a vital role in immune responses at epithelial surfaces. This paper provides an overview of BD-2, shedding light on its structure, function, and therapeutic potential.BD-2 Structure and Function:
BD-2 is a cationic peptide that exhibits a conserved cysteine motif, conferring its antimicrobial activity. It acts by disrupting microbial cell membranes, exerting a broad spectrum of antimicrobial effects against bacteria, fungi, and viruses. Additionally, BD-2 possesses immunomodulatory properties, regulating inflammatory responses and promoting wound healing.Antimicrobial Properties and Therapeutic Applications:
BD-2 demonstrates potent antimicrobial activity against a wide range of pathogens, including drug-resistant strains. Its ability to combat biofilm formation and enhance immune cell recruitment makes it a promising candidate for developing novel antimicrobial therapies. Furthermore, BD-2's immunomodulatory effects hold potential in treating inflammatory disorders.Therapeutic Potential of BD-2 Human Recombinant:
BD-2 human recombinant offers exciting prospects in immunotherapy. Strategies aimed at enhancing BD-2 expression or delivering exogenous BD-2 may boost innate immune responses in individuals with compromised immunity or chronic infections. BD-2-based therapeutics could be developed for wound healing, infectious diseases, and inflammatory conditions.Challenges and Future Directions:
While BD-2 shows great promise, challenges remain. Further research is needed to optimize delivery methods of BD-2 and evaluate its safety and efficacy in clinical settings. Understanding the interplay between BD-2 and other immune factors will enable the development of synergistic therapies for enhanced therapeutic outcomes.Conclusion:
BD-2 human recombinant represents a promising avenue for developing novel immunotherapies and combating antimicrobial resistance. Understanding the molecular mechanisms and functional implications of BD-2 in innate immunity opens new horizons for innovative treatments. Continued research in this field has the potential to revolutionize immunotherapy and improve patient outcomes.What is the molecular weight/Mw of BD2 Protein?
BD2 Protein has a total Mw of 4.3kDa.
What is the source or expression system of BD2 Protein?
Escherichia Coli.
What is the Purity of BD2 Protein?
BD2 Protein is >98% pure as determined by SDS-PAGE.
What is the Biological Activity of BD2 Protein?
Determined by the ability to chemoattract human dendritic immature cells at a concentration of 10-100ng/ml.
What is the amino acid sequence of BD2 Protein?
GIGDPVTCLK SGAICHPVFC PRRYKQIGTC GLPGTKCCKK P.
What applications can BD2 Protein be used in?
BD2 Protein can probably be used in western blot, ELISA and Lateral Flow.
What is the endotoxin level for BD2 Protein?
The endotoxin level is minimal, BD2 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 :
CagrilintideDescription:
Cagrilintide
Product # :
HOR-059Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- formulation
- purity
- More Info
Description
Cagrilintide is a synthetic single, non-glycosylated polypeptide chain containing 37 amino acids, having a molecular mass of 4409 Dalton and a Molecular formula of C194H312N54O59.
Formulation
The protein was lyophilized with no additives.
Purity
Greater than 97.0% as determined by analysis by RP-HPLC.
More Info
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized Cagrilintide although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Cagrilintide 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 Cagrilintide in sterile 18MΩ-cm H2O not less than 100 µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
(Eicosanedioic acid-γ-Glu)-Lys-CysAsn-Thr-Ala-Thr-Cys-Ala-Thr-Gln-Arg-Leu-Ala-Glu-Phe-Leu-Arg-HisSer-Ser-Asn-Asn-Phe-Gly-Pro-Ile-Leu-Pro-Pro-Thr-Asn-Val-Gly-SerAsn-Thr-Pro-NH2 (Disulfide bridge:Cys3-Cys8).
-
Background
Cagrilintide plays a role as a pioneering long-acting amylin analogue and integrates into the fixed-dose combination CagriSema (Cagrilintide + Semaglutide). Unlike GLP-1 agonists, Cagrilintide mimics amylin, a hormone co-secreted with insulin takes part in regulating satiety and slows gastric emptying through brainstem pathways.
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 :
IL34 Human, Sf9Description:
Interleukin 34 Human Recombinant, Sf9
Interleukin-34, IL-34, IL34, C16orf77, Chromosome 16 Open Reading Frame.
Product # :
CYT-1069Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
IL34 produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 231 amino acids (21-242a.a.) and having a molecular mass of 26.3kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).IL34 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Insect cells.
Formulation
IL34 protein solution (0.25mg/ml) contains 20mM Tris-Hcl buffer (pH8.5) 1mM DTT, 0.15M NaCl, 0.1mM PMSF, 1mM EDTA and 30% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
Interleukin 34 (IL34) is a cytokine that promotes the differentiation and viability of monocytes and macrophages through the colony-stimulating factor-1 receptor and is a part of a group of cytokines called interleukins. IL34 increases growth or survival of immune cells known as monocytes. IL34 protein obtains its activity by binding the Colony stimulating factor 1 receptor. Interleukin 34 has also a potential part in viral infection, the adaptive immune response and bone marrow cell proliferation. Furthermore, IL34 plays an important role in innate immunity and in inflammatory processes.
-
Synonyms
Interleukin-34, IL-34, IL34, C16orf77, Chromosome 16 Open Reading Frame.
-
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
ADPNEPLEMW PLTQNEECTV TGFLRDKLQY RSRLQYMKHY FPINYKISVP YEGVFRIANV TRLQRAQVSE RELRYLWVLV SLSATESVQD VLLEGHPSWK YLQEVQTLLL NVQQGLTDVE VSPKVESVLS LLNAPGPNLK LVRPKALLDN CFRVMELLYC SCCKQSSVLN WQDCEVPSPQ SCSPEPSLQY AATQLYPPPP WSPSSPPHST GSVRPVRAQG EGLLPHHHHH 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.
- View Data Sheet
Name :
YOD1 HumanDescription:
YOD1 Human Recombinant
DUBA8, OTUD2, PRO0907, RP11-164O23.1, Ubiquitin thioesterase OTU1, DUBA-8, HIN-7, HsHIN7, OTU domain-containing protein 2.
Product # :
ENZ-696Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
YOD1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 371 amino acids (1-348) and having a molecular mass of 40.7kDa.YOD1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The YOD1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.15M NaCl, 30% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
YOD1 is a Hydrolase which removes conjugated ubiquitin from proteins and takes part in endoplasmic reticulum-associated degradation (ERAD) for misfolded lumenal proteins. YOD1 is a highly conserved deubiquitinating enzyme belonging to the ovarian tumor (otubain) family, whose function has yet to be determined in mammalian cells. YOD1 is a component of a multiprotein complex with p97 as its nucleus, proposing a functional link to a pathway responsible for the dislocation of misfolded proteins from the endoplasmic reticulum. YOD1 variant xpression deprived of its deubiquitinating activity compels a halt on the dislocation reaction, as concluded by the stabilization of various dislocation substrates.
-
Synonyms
DUBA8, OTUD2, PRO0907, RP11-164O23.1, Ubiquitin thioesterase OTU1, DUBA-8, HIN-7, HsHIN7, OTU domain-containing protein 2.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMFGPAKG RHFGVHPAPG FPGGVSQQAA GTKAGPAGAW PVGSRTDTMW RLRCKAKDGT HVLQGLSSRT RVRELQGQIA AITGIAPGGQ RILVGYPPEC LDLSNGDTIL EDLPIQSGDM LIIEEDQTRP RSSPAFTKRG ASSYVRETLP VLTRTVVPAD NSCLFTSVYY VVEGGVLNPA CAPEMRRLIA QIVASDPDFY SEAILGKTNQ EYCDWIKRDD TWGGAIEISI LSKFYQCEIC VVDTQTVRID RFGEDAGYTK RVLLIYDGIH YDPLQRNFPD PDTPPLTIFS SNDDIVLVQA LELADEARRR RQFTDVNRFT LRCMVCQKGL TGQAEAREHA KETGHTNFGE 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.
- View Data Sheet
Name :
tPA Human, Sf9Description:
Tissue Plasminogen Activator Human Recombinant, Sf9
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
Product # :
ENZ-1011Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
tPA Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 545 amino acids (24-562 a.a) and having a molecular mass of 61.3kDa (Molecular size on SDS-PAGE will appear at approximately 50-70kDa).tPA is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
tPA protein solution (0.25mg/ml) containing 50mM MES buffer(pH 5.5 ), 40% glycerol, 5mM CaCl2, 1mM DTT and 0.5M NaCl.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Tissue plasminogen activator (abbreviated PLAT or tPA) is a secreted serine proteasewhich converts the proenzymeplasminogento plasmin, a fibrinolyticenzyme. Plasminogen is synthesized as a single chain which is cleaved by PLAT into the two chain disulfide linked plasmin.
This enzyme plays a role in cell migrationand tissue remodeling. Increased enzymatic activity causes hyperfibrinolysis, which manifests as excessive bleeding; decreased activity leads to hypofibrinolysiswhich can result in thrombosisor embolism. -
Synonyms
Tissue-type plasminogen activator, EC 3.4.21.68, tPA, t-PA, t-plasminogen activator, TPA, T-PA, DKFZp686I03148, PLAT and tPA.
-
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
QEIHARFRRG ARSYQVICRD EKTQMIYQQH QSWLRPVLRS NRVEYCWCNS GRAQCHSVPV KSCSEPRCFN GGTCQQALYF SDFVCQCPEG FAGKCCEIDT RATCYEDQGI SYRGTWSTAE SGAECTNWNS SALAQKPYSG RRPDAIRLGL GNHNYCRNPD RDSKPWCYVF KAGKYSSEFC STPACSEGNS DCYFGNGSAY RGTHSLTESG ASCLPWNSMI LIGKVYTAQN PSAQALGLGK HNYCRNPDGD AKPWCHVLKN RRLTWEYCDV PSCSTCGLRQ YSQPQFRIKG GLFADIASHP WQAAIFAKHR RSPGERFLCG GILISSCWIL SAAHCFQERF PPHHLTVILG RTYRVVPGEE EQKFEVEKYI VHKEFDDDTY DNDIALLQLK SDSSRCAQES SVVRTVCLPP ADLQLPDWTE CELSGYGKHE ALSPFYSERL KEAHVRLYPS SRCTSQHLLN RTVTDNMLCA GDTRSGGPQA NLHDACQGDS GGPLVCLNDG RMTLVGIISW GLGCGQKDVP GVYTKVTNYL DWIRDNMRPHHHHHH.
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 :
IL 22 Mouse, PEGDescription:
Interleukin-22 Mouse Recombinant, Pegylated
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
Product # :
CYT-701Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- biological activity
- More Info
Description
Pegylated Interleukin-22 Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and an aditional Ala amino acid at N-terminus having a molecular mass of 36 kDa as determioned by mass spectometry. However due to enlarged hydrodymanic volume it runs on the SDS-PAGE as a 50 kDa protein and in gel-filtration on Superdex 200 as over 200 kDa protein. The Murine IL-22 is Mono-pegylated (with 20 kDa PEG) purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Lyophilized from a concentrated solution at 0.65mg/ml containing 0.003mM NaHCO3.
Purity
Greater than 98.0% as determined by:
(a) Analysis by Gel-Filtration.
(b) Analysis by SDS-PAGE.Biological Activity
The ED50 as determined by STAT3 phosphorylation assay in HepG cells. The activity in vitro was found to be ~ 10% compared to the non-pegylated mouse IL22.More Info
-
Introduction
Interleukin-22 (IL-22), also known as IL-10-related T cell-derived inducible factor (IL-TIF) was initially identified as a gene induced by IL-9 in mouse T cells and mast cells. Mouse IL-22 cDNA encodes a 179 amino acid residue protein with a putative 33 amino acids signal peptide that is cleaved to generate a 147 aa mature protein that shares approximately 79% and 22% aa sequence identity with human IL-22 and IL-10, respectively. IL-22 has been shown to activate STAT-1 and STAT-3 in several hepatoma cell lines and upregulate the production of acute phase proteins. IL-22 is produced by normal mouse T cells upon Con A activation. Mouse IL-22 expression is also induced in various organs upon lipopolysaccharide injection, suggesting that IL-22 may be involved in inflammatory responses. The functional IL-22 receptor complex consists of two receptor subunits, IL-22R (previously an orphan receptor named CRF2-9) and IL-10Rβ (previously known as CRF2-4), belonging to the class II cytokine recep
-
Synonyms
IL-TIF, TIFa, IL-10-related T-cell-derived-inducible factor, IL-22, ILTIF, IL-D110, zcyto18, MGC79382, MGC79384, TIFIL-23.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized pegylated murine IL22 although stable at room temperature for several days, should be stored desiccated below -20°C. Upon reconstitution at 0.1mg/ml pegylated mouse IL22 and up to 2mg/ml, filter and sterilized, the protein can be stored at 4 degrees Celsius 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 mouse Interleukin -22 in sterile 0.4% NaHCO3 adjusted to pH 8-9 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.
- View Data Sheet
Name :
SYT11 HumanDescription:
Synaptotagmin XI Human Recombinant
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
Product # :
PRO-2301Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SYT11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 418 amino acids (37-431 a.a) and having a molecular mass of 47kDa. SYT11 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
E.coli.
Formulation
SYT11 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH7.4) and 50% glycerol.
Purity
Greater than 80% as determined by SDS-PAGE.
More Info
-
Introduction
Synaptotagmin-11 (SYT11) protein may be involved in Ca2+-dependent exocytosis of secretory vesicles through Ca2+ and phospholipid binding to the C2 domain or may function as Ca2+ sensors in the process of vesicular trafficking and exocytosis.
-
Synonyms
Synaptotagmin XI, SytXI, Synaptotagmin 12, KIAA0080, SYT12, Synaptotagmin-11.
-
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 MGSWSCCHQQ AEKKQKNPPY KFIHMLKGIS IYPETLSNKK KIIKVRRDKD GPGREGGRRN LLVDAAEAGL LSRDKDPRGP SSGSCIDQLP IKMDYGEELR SPITSLTPGE SKTTSPSSPE EDVMLGSLTF SVDYNFPKKA LVVTIQEAHG LPVMDDQTQG SDPYIKMTIL PDKRHRVKTR VLRKTLDPVF DETFTFYGIP YSQLQDLVLH FLVLSFDRFS RDDVIGEVMV PLAGVDPSTG KVQLTRDIIK RNIQKCISRG ELQVSLSYQP VAQRMTVVVL KARHLPKMDI TGLSGNPYVK VNVYYGRKRI AKKKTHVKKC TLNPIFNESF IYDIPTDLLP DISIEFLVID FDRTTKNEVV GRLILGAHSV TASGAEHWRE VCESPRKPVA KWHSLSEY.
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 :
AHCY Human, Sf9Description:
Adenosylhomocysteinase Human Recombinant, Sf9
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
Product # :
ENZ-1034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
AHCY Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 441 amino acids (1-432 a.a.) and having a molecular mass of 48.8kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions). AHCY is fused to a 6 amino acids His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
AHCY protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90% as determined by SDS-PAGE.
More Info
-
Introduction
AHCY is an enzyme that catalyzes the reversible hydrolysis of S-adenosylhomocysteine (AdoHcy) to adenosine (Ado) and L-homocysteine (Hcy). AHCY controls the intracellular S-adenosylhomocysteine (SAH) concentration that is crucial for transmethylation reactions. AHCY deficiency causes hypermethioninemia.
-
Synonyms
EC 3.3.1.1, SAHH, AdoHcyase, S-adenosyl-L-homocysteine hydrolase, AHCY, Adenosylhomocysteinase.
-
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
ADLMSDKLPY KVADIGLAAW GRKALDIAEN EMPGLMRMRE RYSASKPLKG ARIAGCLHMT VETAVLIETL VTLGAEVQWS SCNIFSTQDH AAAAIAKAGI PVYAWKGETD EEYLWCIEQT LYFKDGPLNM ILDDGGDLTN LIHTKYPQLL PGIRGISEET TTGVHNLYKM MANGILKVPA INVNDSVTKS KFDNLYGCRE SLIDGIKRAT DVMIAGKVAV VAGYGDVGKG CAQALRGFGA RVIITEIDPI NALQAAMEGY EVTTMDEACQ EGNIFVTTTG CIDIILGRHF EQMKDDAIVC NIGHFDVEID VKWLNENAVE KVNIKPQVDR YRLKNGRRII LLAEGRLVNL GCAMGHPSFV MSNSFTNQVM AQIELWTHPD KYPVGVHFLP KKLDEAVAEA HLGKLNVKLT KLTEKQAQYL GMSCDGPFKP DHYRYHHHHH H.
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
- View Data Sheet
Name :
SDF2 Human, sf9Description:
Stromal Cell-Derived Factor 2, Sf9 Human Recombinant
Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2
Product # :
CHM-034Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
SDF2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 202 amino acids (19-211a.a.) and having a molecular mass of 22.3kDa. (Molecular size on SDS-PAGE will appear at approximately 18-28kDa). SDF2 is expressed with an 9 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
SDF2 protein solution (0.25mg/ml) contains 50mM Tris-HCl (pH 8.0), 10% glycerol, 0.1M NaCl 0.1mM PMSF and 0.5mM EDTA.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Stromal Cell-Derived Factor 2 (SDF2) is a secretory protein which is partly similar to the hydrophilic segments of yeast mannosyltransferases. SDF2 protein’s expression is ubiquitous and the gene is rather conserved among mammals. SDF2 is a protein-coding gene whose alternative splicing results in coding and non-coding variants.
-
Synonyms
Stromal Cell Derived Factor 2, Stromal Cell-Derived Factor 2, SDF-2
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
ADPSSLGVVT CGSVVKLLNT RHNVRLHSHD VRYGSGSGQQ SVTGVTSVDD SNSYWRIRGK SATVCERGTP IKCGQPIRLT HVNTGRNLHS HHFTSPLSGN QEVSAFGEEG EGDYLDDWTV LCNGPYWVRD GEVRFKHSST EVLLSVTGEQ YGRPISGQKE VHGMAQPSQN NYWKAMEGIF MKPSELLKAE AHHAELHHHH 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 :
NREP HumanDescription:
Neuronal Regeneration Related Protein Human Recombinant
Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.
Product # :
PRO-1780Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
NREP Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 91 amino acids (1-68) and having a molecular mass of 10.3kDa.NREP is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The NREP solution (0.5mg/ml) contains 20mM Tris-HCl buffer (pH8.0), 10% glycerol and 0.1M NaCl.
Purity
Greater than 85.0% as determined by SDS-PAGE.
More Info
-
Introduction
Neuronal Regeneration Related Protein (NREP) has roles in neural function. NREP promotes axonal regeneration. In addition, NREP has functions in cellular differentiation. NREP protein induces differentiation of fibroblast into myofibroblast and increases retinoic-acid regulation of lipid-droplet biogenesis. NREP down-regulates the expression of TGFB1 and TGFB2 but not of TGFB3. NREP has a role in the regulation of alveolar generation.
-
Synonyms
Neuronal regeneration-related protein, Neuronal protein 3.1, Protein p311, NREP, C5orf13, P311, PTZ17, Chromosome 5 Open Reading Frame 13, Neuronal Regeneration Related Protein Homolog (Rat), D4S114, PRO1873, SEZ17, Neuronal Regeneration Related Protein Homolog, Neuronal Regeneration-Related Protein.
-
Physical Appearance
Sterile Filtered colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMVYYPEL FVWVSQEPFP NKDMEGRLPK GRLPVPKEVN RKKNDETNAA SLTPLGSSEL RSPRISYLHF F.
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 :
BASP1 HumanDescription:
Brain Abundant Membrane Attached Signal Protein 1 Human Recombinant
CAP-23, CAP23, NAP-22, NAP22, Brain acid soluble protein 1, BASP1, BASP1 Human, 22 kDa neuronal tissue-enriched acidic protein, Neuronal axonal membrane protein NAP-22.
Product # :
PRO-1355Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
BASP1 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 250 amino acids (1-227) and having a molecular mass of 25 kDa (Molecular size on SDS-PAGE will appear higher). BASP1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
The BASP1 solution (0.25mg/ml) contains 20mM Tris-HCl buffer (pH 8.0), 0.2M NaCl and 20% glycerol.
Purity
Greater than 95.0% as determined by SDS-PAGE.
More Info
-
Introduction
Brain Abundant Membrane Attached Signal Protein 1 (BASP1) is a membrane bound protein with numerous transient phosphorylation positions and PEST motifs. Preservation of proteins with PEST sequences amongst diverse species supports their functional significance. PEST sequences take place in proteins with high turnover rates. Immunological attributes of this protein are species specific. BASP1 undergoes N-terminal myristoylation.
-
Synonyms
CAP-23, CAP23, NAP-22, NAP22, Brain acid soluble protein 1, BASP1, BASP1 Human, 22 kDa neuronal tissue-enriched acidic protein, Neuronal axonal membrane protein NAP-22.
-
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 MGSMGGKLSK KKKGYNVNDE KAKEKDKKAE GAATEEEGTP KESEPQAAAE PAEAKEGKEK PDQDAEGKAE EKEGEKDAAA AKEEAPKAEP EKTEGAAEAK AEPPKAPEQE QAAPGPAAGG EAPKAAEAAA APAESAAPAA GEEPSKEEGE PKKTEAPAAP AAQETKSDGA PASDSKPGSS EAAPSSKETP AATEAPSSTP KAQGPAASAE EPKPVEAPAA NSDQTVTVKE.
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 :
CDK5 Human, Sf9Description:
Cyclin-Dependent Kinase 5 Human Recombinant,Sf9
CDK5, Cyclin Dependent Kinase 5, Serine/Threonine-Protein Kinase PSSALRE, Tau Protein Kinase II Catalytic Subunit, Cell Division Protein Kinase 5, TPKII Catalytic Subunit, Cyclin-Dependent-Like Kinase 5, Protein Kinase CDK5 Splicing, EC 2.7.11.22, EC 2.7.11.1, EC 2.7.11, PSSALRE, CDKN5, LIS7.
Product # :
PKA-104Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CDK5 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 298 amino acids (1-292a.a.) and having a molecular mass of 34.1kDa. (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).CDK5 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CDK5 protein solution (0.25mg/ml) Phosphate Buffered Saline (pH 7.4) containing 40% glycerol and 1mM DTT.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Cell division protein kinase 5 (CDK5) belongs to the cyclin-dependent kinase family. CDK5 is essential for appropriate development of the brain and in order to be activated CDK5 must link to CDK5R1 or CDK5R2. CDK5 doesn't need phosphorylation on the T loop so that binding with the activator is enough to activate the kinase. CDK5 is engaged in the processes of neuronal maturation and migration, phosphorylating the central intracellular adaptor of the reeling signaling chain.
-
Synonyms
CDK5, Cyclin Dependent Kinase 5, Serine/Threonine-Protein Kinase PSSALRE, Tau Protein Kinase II Catalytic Subunit, Cell Division Protein Kinase 5, TPKII Catalytic Subunit, Cyclin-Dependent-Like Kinase 5, Protein Kinase CDK5 Splicing, EC 2.7.11.22, EC 2.7.11.1, EC 2.7.11, PSSALRE, CDKN5, LIS7.
-
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
MQKYEKLEKI GEGTYGTVFK AKNRETHEIV ALKRVRLDDD DEGVPSSALR EICLLKELKH KNIVRLHDVL HSDKKLTLVF EFCDQDLKKY FDSCNGDLDP EIVKSFLFQL LKGLGFCHSR NVLHRDLKPQ NLLINRNGEL KLADFGLARA FGIPVRCYSA EVVTLWYRPP DVLFGAKLYS TSIDMWSAGC IFAELANAGR PLFPGNDVDD QLKRIFRLLG TPTEEQWPSM TKLPDYKPYP MYPATTSLVN VVPKLNATGR DLLQNLLKCN PVQRISAEEA LQHPYFSDFC PPHHHHHH
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 :
ProInsulin HumanDescription:
ProInsulin C-Peptide Analogue Human Recombinant
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
Product # :
CYT-1120Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
ProInsulin C-Peptide Analogue Human Recombinant produced in E.Coli is a non-glycosylated polypeptide chain containing 35 amino acid and having a molecular mass of approximately 3.6kDa.ProInsulin 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 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.More Info
-
Introduction
Insulin decreases blood glucose concentration. Insulin increases cell permeability to monosaccharides, amino acids and fatty acids. Insulin accelerates glycolysis, the pentose phosphate cycle, and glycogen synthesis in liver.
-
Synonyms
Insulin, Insulin-Dependent Diabetes Mellitus 2, Preproinsulin, Proinsulin, MODY10, IDDM1, IDDM2, IDDM, ILPR, IRDN.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized ProInsulin although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution ProInsulin C-Peptide Analogue should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.
-
Solubility
It is recommended to reconstitute the lyophilized ProInsulin C-Peptide Analogue in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Amino Acid Sequence
RREAEDLQVG QVELGGGPGA GSLQPLALEG SLQKR.
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 :
CLEC5A Human, Sf9Description:
C-Type Lectin Domain Family 5, Member A Human Recombinant, Sf9
C-type lectin domain family 5 member A , CLECSF5, MDL-1, MDL1, C-type lectin superfamily member 5, Myeloid DAP12-associating lectin 1.
Product # :
PRO-2554Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
CLEC5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (28-188 a.a.) and fused to a 9 aa His Tag at C-terminus containing a total of 170 amino acids and having a molecular mass of 19.5kDa.CLEC5A shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
CLEC5A protein solution (0.25mg/ml) contains 20% glycerol, 1mM DTT & Phosphate buffered saline (pH7.4).
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
C-type lectin domain family 5-member A isoform 1 (CLEC5A) is part of the CTL/CTLD superfamily which carry various functions, for instance cell-cell signaling, cell adhesion, glycoprotein turnover, in addition to their inflammation & immune response abilities. CLEC5A operates as a cell attachment receptor for all 4 serotypes of Dengue virus in addition to Japanese encephalitis virus. CLEC5A binds to the dengue virus and it triggers signaling through the phosphylation of TYROBP, as a result no viral entrance occurs, however this interaction does stimulate proinflammatory cytokine release. CLEC5A preforms as a positive regulator of osteoclastogenesis and also a main regulator of synovial injury & bone erosion for the period of autoimmune joint inflammation.
-
Synonyms
C-type lectin domain family 5 member A , CLECSF5, MDL-1, MDL1, C-type lectin superfamily member 5, Myeloid DAP12-associating lectin 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
ADLPQIFNKS NDGFTTTRSY GTVSQIFGSS SPSPNGFITT RSYGTVCPKD WEFYQARCFF LSTSESSWNE SRDFCKGKGS TLAIVNTPEK LKFLQDITDA EKYFIGLIYH REEKRWRWIN NSVFNGNVTN QNQNFNCATI GLTKTFDAAS CDISYRRICE KNAKHHHHHH
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 :
GZMH Human, sf9Description:
Granzyme-H Human Recombinant, sf9
Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.
Product # :
ENZ-961Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
GZMH produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 234 amino acids (19-246 a.a.) and having a molecular mass of 26.2kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa). GZMH is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
GZMH protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Granzyme H also known as GZMH belongs to the peptidase S1 family. GZMH is an essential part for HBV eradication. The HBx protein, which is required for the replication of HBV, is cleaved at Met(79) by GZMH. Furthermore, GZMH inhibitor can abolish GZNH- as well as lymphokine-activated killer cell-mediated HBx degradation and HBV clearance. A HBx-deficient HBV is resistant to GzmH- in addition to lymphokine-activated killer cell-mediated viral clearance.
-
Synonyms
Granzyme H, Granzyme H (Cathepsin G-Like 2, Protein H-CCPX), Cytotoxic T-Lymphocyte Proteinase, Cathepsin G-Like 2, CTSGL2, CCP-X, CSP-C, Cytotoxic T-Lymphocyte-Associated Serine Esterase 1, Cathepsin G-Like 2, Protein H-CCPX, Cytotoxin Serine Protease-C, Cytotoxic Serine Protease C, Protein H-CCPX, EC 3.4.21.79, EC 3.4.21, EC 3.4.21, CTLA1, CGL-2 , CGL2.
-
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
EEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPPGV YIKVSHFLPW IKRTMKRLHH 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 :
SPP1 HumanDescription:
Osteopontin Human Recombinant
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
Product # :
CYT-635Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
Secreted Phosphoprotein-1 Human Recombinant produced in E.Coli is single, a non-glycosylated, Polypeptide chain containing 321 amino acids fragment (17-314) and having a total molecular mass of 36.2 kDa(molecular weight on SDS-PAGE will shift up). The SPP1 protein is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Source
Escherichia Coli.
Formulation
Osteopontin is supplied in 20mM Tris-HCl buffer pH-7.5, 1mM DTT, 2mM EDTA and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Osteopontin is a glycoprotein that was first identified in osteoblasts and is involved in bone remodeling, immune functions in fibroblasts, macrophages, and lymphocytes during inflammation and wound healing. SPP1 binds tightly to hydroxyapatite. SPP1 forms an integral part of the mineralized matrix. SPP1 is vital to cell-matrix interaction.
Secreted Phosphoprotein-1 protects against cardiac ischemia-reperfusion injury via late preconditioning. Expression of both Ostepontin and CD44 in hepatocellular carcinoma is linked with advanced tumor stage and contributes to prognosis information. SPP1 is the most over-expressed gene in intrahepatic cholangiocarcinoma. Secreted Phosphoprotein-1 overexpression is related with interstitial lung diseases. -
Synonyms
Secreted Phosphoprotein-1, OPN, BNSP, BSPI, ETA-1, MGC110940, SPP-1, Osteopontin, Bone sialoprotein 1, Urinary stone protein, Nephropontin, Uropontin, SPP1.
-
Physical Appearance
Sterile Filtered clear colorless solution.
-
Stability
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.
-
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH RSMIPVKQAD SGSSEEKQLY NKYPDAVATW LNPDPSQKQN LLAPQNAVSS EETNDFKQET LPSKSNESHD HMDDMDDEDD DDHVDSQDSI DSNDSDDVDD TDDSHQSDES HHSDESDELV TDFPTDLPAT EVFTPVVPTV DTYDGRGDSV VYGLRSKSKK FRRPDIQYPD ATDEDITSHM ESEELNGAYK AIPVAQDLNA PSDWDSRGKD SYETSQLDDQ SAETHSHKQS RLYKRKANDE SNEHSDVIDS QELSKVSREF HSHEFHSHED MLVVDPKSKE EDKHLKFRIS HELDSASSEV N.
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 :
LY9 HumanDescription:
Lymphocyte Antigen 9 Human Recombinant
Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.
Product # :
PRO-2338Price :
Quantity :
Shipping Method :
Shipped with Ice Packs
More Info
- description
- source
- formulation
- purity
- More Info
Description
LY9 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 416 amino acids (48-454 aa) and having a molecular mass of 45.9kDa (Migrates at 40-57kDa on SDS-PAGE under reducing conditions).LY9 is expressed with a 6 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Source
Sf9, Baculovirus cells.
Formulation
LY9 protein solution (0.25mg/ml) containing Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Purity
Greater than 90.0% as determined by SDS-PAGE.
More Info
-
Introduction
Lymphocyte Antigen 9, also known as LY9 is a member of the SLAM family of immunomodulatory receptors, LY9 interacts with the adaptor molecule SAP . LY9 plays a part in adhesion reactions between T lymphocytes and accessory cells via homophilic interaction. LY9 promotes T-cell differentiation into a helper T-cell Th17 phenotype which leads to increased IL-17 secretion; the costimulatory activity requires SH2D1A. Furthermore it also promotes recruitment of RORC to the IL-17 promoter. LY9 is implicated in the maintenance of peripheral cell tolerance through serving as a negative regulator of the immune response. LY9 disables autoantibody responses as well as inhibits IFN-gamma secretion by CD4(+) T-cells. Moreover, LY9 negatively regulate the size of thymic innate CD8(+) T-cells and the development of invariant natural killer T (iNKT) cells. Systemic Lupus Erythematosus is one of the diseases which are associated with LY9.
-
Synonyms
Lymphocyte Antigen 9, Signaling Lymphocytic Activation Molecule 3, Cell Surface Molecule Ly-9, SLAM Family Member 3, SLAMF3, CD229 Antigen, CD229, Hly9, MLY9, LY9.
-
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
ADLKDSAPTV VSGILGGSVT LPLNISVDTE IENVIWIGPK NALAFARPKE NVTIMVKSYL GRLDITKWSY SLCISNLTLN DAGSYKAQIN QRNFEVTTEE EFTLFVYEQL QEPQVTMKSV KVSENFSCNI TLMCSVKGAE KSVLYSWTPR EPHASESNGG SILTVSRTPC DPDLPYICTA QNPVSQRSSL PVHVGQFCTD PGASRGGTTG ETVVGVLGEP VTLPLALPAC RDTEKVVWLF NTSIISKERE EAATADPLIK SRDPYKNRVW VSSQDCSLKI SQLKIEDAGP YHAYVCSEAS SVTSMTHVTL LIYRRLRKPK ITWSLRHSED GICRISLTCS VEDGGNTVMY TWTPLQKEAV VSQGESHLNV SWRSSENHPN LTCTASNPVS RSSHQFLSEN ICSGPERNTK HHHHHH
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 :
LTF Apo HumanDescription:
Lactoferrin Apo Human Recombinant
Lactotransferrin, Lactoferrin, Growth-inhibiting protein 12, Talalactoferrin, LTF, GIG12, LF, HLF2, Neutrophil Lactoferrin.
Product # :
PRO-2771Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- description
- source
- formulation
- purity
- More Info
Description
Recombinant Human Apo Lactoferrin produced in Plant is a glycosylated mature polypeptide sequence having an approximate molecular mass of 80 kDa.The Human Apo Lactoferrin is purified by proprietary chromatographic techniques.
Source
Rice Flour.
Formulation
The Human Apo lactoferrin was lyophilized with no additives.
Purity
Greater than 95% as determined by SDS-PAGE.
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 Apo Lactoferrin although stable at room temperature for 3 weeks, should be stored 2-8°C.
-
Solubility
It is recommended to reconstitute the lyophilized LTF Apo 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.
- View Data Sheet
Name :
CALM BovineDescription:
Calmodulin Bovine
Calmodulin, CaM, CALM.
Product # :
PRO-2800Price :
Quantity :
Shipping Method :
Shipped at Room temp
More Info
- source
- formulation
- purity
- More Info
Source
Bovine brain tissue.
Formulation
CALM was lyophilized with 2mM EDTA.
Purity
Greater than 95.0%.
More Info
-
Synonyms
Calmodulin, CaM, CALM.
-
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
-
Stability
Lyophilized CALM although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution Calmodulin 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 CALM in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
-
Applications
Biochemical and immunochemical investigations.
-
Background
Role in Muscle Contraction and Relaxation:
In muscle cells, calmodulin plays a pivotal role in the regulation of contraction and relaxation. It interacts with myosin light-chain kinase during muscle contraction, initiating the process of cross-bridge cycling. Conversely, during muscle relaxation, calmodulin activates the enzyme myosin light-chain phosphatase, leading to the dephosphorylation of myosin and muscle relaxation. This delicate balance is crucial for proper muscle function.
Neuronal Signalling and Synaptic Plasticity:
In neurons, calmodulin is essential for neurotransmitter release and synaptic plasticity. It modulates the activity of proteins involved in vesicle fusion and neurotransmitter release. Additionally, calmodulin-dependent protein kinases (CaMKs) are critical for synaptic plasticity, learning, and memory. The intricate interplay between calmodulin and neuronal proteins underpins the fundamental processes of learning and cognition.
Implications in Disease and Therapeutics:
Dysregulation of calmodulin has been implicated in various diseases, including cardiac arrhythmias and neurodegenerative disorders. Mutations in calmodulin genes can lead to aberrant calcium signalling and cellular dysfunction. Consequently, understanding these molecular mechanisms offers potential therapeutic targets. Researchers are exploring calmodulin inhibitors and modulators for conditions like cardiac arrhythmias, aiming to restore normal cellular function.
Conclusion:
Calmodulin, with its remarkable structural versatility and central role in cellular signalling, epitomizes the complexity of biological regulation. Its influence spans from the fundamental processes of muscle contraction to the intricacies of neuronal signalling. Unravelling the mysteries of calmodulin not only deepens our understanding of basic biological phenomena but also holds the promise of innovative therapeutic interventions. This research illuminates calmodulin's significance, emphasizing its position as a master regulator in the orchestra of cellular life.
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.